Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Application Status
This application is a CON of PCT/US2020/070440, filed on 01/24/2022.
Claims 1-5, 7-20 are currently pending in the instant patent application.
In response to a previous Office action, a Non-Final Rejection Office action (mailed on 07/02/2025), Applicants filed a response and an amendment on 12/18/2025, amending claims 1, 7-9, and canceling claim 6 is acknowledged.
Claims 1-5, and 7-20 are present for examination.
Applicants' arguments filed on 12/18/2025, have been fully considered and are deemed persuasive to overcome some of the rejections previously applied. Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.
Priority
Acknowledgement is made of applicants claim for priority of US Provisional application, 62/890,641, filed on 08/23/2019, and International patent application PCT/US2020/070440, filed on 08/21/2020.
Maintained-Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The previous rejection of Claims 1-5, 7-19 and 20 under 35 U.S.C. 112(b), as being indefinite and vague for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention, is maintained. This rejection has been discussed at length in the previous Office Action, and the rejection is maintained as discussed previously and for the following reasons.
Claim 1, b) is indefinite in the recitation “collagen inhibiting gene” in the context of reduced amount of collagen synthesis in the fibroblast by an agent, compound, gene encoding protein, peptide, which is confusing. The Metes and Bounds of the term are not clear to the Examiner. The phrase is defined in the specification by non-limiting examples, and extremely confusing of the term “inhibiting” conjunction with “collagen” and “gene”, because claimed invention is- identifying an agent that inhibits collage synthesis, and the target should be collagen synthesis genes, and that agent can be compound, DNA, RNA, siRNA, micro-RNA, peptide, or protein, and thus, said words encompasses many things, which are unknown rendering the Metes and Bounds of the term unclear, confusing and indefinite. Besides, the “collagen inhibiting genes” are not commensurate with the scope of the invention. Furthermore, the claimed invention is drawn to using any collagen synthesis genes for the synthesis of collagen, or any agents like, DNA, RNA, siRNA, micro-RNA, compounds, proteins or peptides, which inhibits collagen synthesis in the fibroblast, which are unknown, rendering the metes and bounds of the term unclear. Claims 2-5 and 7-20 are also rejected as they depend directly or indirectly on claim 1. Clarification and corrections are required.
Arguments: Applicants argue that the specification at page 8, lines 6-7, states that collagen inhibiting gene refers to human genes of interest that inhibit collagen synthesis, and are listed in Fig. 6, and Applicants assert that the recitation collagen inhibiting gene is not indefinite.
Response: This is not found persuasive because collagen inhibiting genes are listed Fig. 6 contains SMAD4 gene as collagen inhibiting gene. However, it is well known that SMAD4 gene encoding SMAD4 protein regarded as collagen synthesizing gene (see, Evidential reference: Yu et al. (Smad4-dependent regulation of type I collagen expression in the muscle of grass carp fed with faba bean. Gene 685 (2019, Epub 10/26/2018): 32-41), but not as collagen inhibiting gene (see, Fig. 8 of Yu et al. as shown below). Therefore, the rejection is maintained.
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Withdrawn-Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The previous rejection of Claims 1-20 under 35 U.S.C. 1112(b), as being indefinite and vague for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention, is withdrawn, in view of Applicant’s amendment to the claims and persuasive arguments.
The previous rejection of Claims 1-20 under 35 U.S.C. 112(b), second paragraph, as being indefinite and vague for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention, is withdrawn, in view of Applicant’s amendment to the claims and persuasive arguments.
The previous rejection of Claims 1-20 are rejected under 35 U.S.C. 112(b), as being indefinite and vague for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention, is withdrawn, in view of Applicant’s amendment to the claims and persuasive arguments.
The previous rejection of Claim 17 is rejected under 35 U.S.C. 112(b) or second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention, is withdrawn, in view of Applicant’s amendment to the claims and persuasive arguments.
The previous rejection of Claim 8 under 35 U.S.C. 112(b), as being indefinite and vague for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention, is withdrawn, in view of Applicant’s amendment to the claims and persuasive arguments.
Withdrawn-Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless -
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
MPEP-2131 Anticipation — Application of 35 U.S.C. 102 [R-08.2017]
A claimed invention may be rejected under 35 U.S.C. 102 when the invention is anticipated (or is "not novel") over a disclosure that is available as prior art. To reject a claim as anticipated by a reference, the disclosure must teach every element required by the claim under its broadest reasonable interpretation. See, e.g., MPEP § 2114, subsections II and IV.
"A claim is anticipated only if each and every element as set forth in the claim is found, either expressly or inherently described, in a single prior art reference." Verdegaal Bros. v. Union Oil Co. of California, 814 F.2d 628, 631, 2 USPQ2d 1051, 1053 (Fed. Cir. 1987). "When a claim covers several structures or compositions, either generically or as alternatives, the claim is deemed anticipated if any of the structures or compositions within the scope of the claim is known in the prior art." Brown v. 3M, 265 F.3d 1349, 1351, 60 USPQ2d 1375, 1376 (Fed. Cir. 2001) Note that, in some circumstances, it is permissible to use multiple references in a 35 U.S.C. 102 rejection. See MPEP § 2131.01.
MPEP-2131.01 Multiple Reference 35 U.S.C. 102 Rejections [R-11.2013]
Normally, only one reference should be used in making a rejection under 35 U.S.C. 102. However, a 35 U.S.C. 102 rejection over multiple references has been held to be proper when the extra references are cited to:
(A) Prove the primary reference contains an "enabled disclosure;"
(B) Explain the meaning of a term used in the primary reference; or
(C) Show that a characteristic not disclosed in the reference is inherent.
The previous rejection of Claims 1-2, 6-7, 8, and 16 under 35 U.S.C. 102(a)(1) based upon a public use or sale or other public availability of the invention as anticipated by Bagchi et al. (Development of a high throughput luciferase gene system for screening activators and repressors of human collagen I-alpha2 gene expression. NRC Research Press. Can J Physiol. Pharmocol. (2015), 93: 887-892, see IDS), is withdrawn because the ref does not teach protein production or transcriptome analysis, but indeed teach luciferase analysis, in view of Applicant’s amendment to the claims and persuasive arguments.
Withdrawn-Claim Rejections - 35 U.S.C. § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
According to MPEP 2143:
“Exemplary rationales that may support a conclusion of obviousness include:
(A) Combining prior art elements according to known methods to yield
predictable results;
(B) Simple substitution of one known element for another to obtain predictable
results;
(C) Use of known technique to improve similar devices (methods, or products)
in the same way;
(D) Applying a known technique to a known device (method, or product) ready
for improvement to yield predictable results;
(E) “ Obvious to try ” – choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success;
(F) Known work in one field of endeavor may prompt variations of it for use in
either the same field or a different one based on design incentives or other market
forces if the variations are predictable to one of ordinary skill in the art;
(G) Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art
reference teachings to arrive at the claimed invention.
Note that the list of rationales provided is not intended to be an all-inclusive list. Other rationales to support a conclusion of obviousness may be relied upon by Office personnel.”
The previous rejection of Claims 1-2, 3-5, 6-7, 8-15, 16, 17-19 and 20 under 35 U.S.C. 103 as being unpatentable over Bagchi et al. (Development of a high throughput luciferase gene system for screening activators and repressors of human collagen I-alpha2 gene expression. NRC Research Press. Can J Physiol. Pharmocol. (2015), 93: 887-892, see IDS) in view of Granstein et al. (Interferons and collagen production. J. Invest Dermatol. (1990), 95(6): 75S-80S), Duisters et al. (miR-133 and miR-30 Regulate Connective Tissue Growth Factor- Implications for a Role of MicroRNAs in Myocardial Matrix Remodeling. Circulation Research (2009), 140: 170-178), Aper et al. (Colorful protein based fluorescent probes for collagen imaging. PLOS ONE (2014), 9(12): e114983, p1-21), and Sullivan et a. (Medical devices incorporating collagen inhibitors: US 2008/0132941A1, publication 06/05/2008), is withdrawn because the ref does not teach protein production or transcriptome analysis, but indeed teach luciferase analysis, in view of Applicant’s amendment to the claims and persuasive arguments.
New-Claim Rejections - 35 U.S.C. § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
According to MPEP 2143:
“Exemplary rationales that may support a conclusion of obviousness include:
(A) Combining prior art elements according to known methods to yield
predictable results;
(B) Simple substitution of one known element for another to obtain predictable
results;
(C) Use of known technique to improve similar devices (methods, or products)
in the same way;
(D) Applying a known technique to a known device (method, or product) ready
for improvement to yield predictable results;
(E) “ Obvious to try ” – choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success;
(F) Known work in one field of endeavor may prompt variations of it for use in
either the same field or a different one based on design incentives or other market
forces if the variations are predictable to one of ordinary skill in the art;
(G) Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art
reference teachings to arrive at the claimed invention.
Note that the list of rationales provided is not intended to be an all-inclusive list. Other rationales to support a conclusion of obviousness may be relied upon by Office personnel.”
Claims 1-2, 3-5, 7, 8-15, 16, 17-19 and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Bagchi et al. (Development of a high throughput luciferase gene system for screening activators and repressors of human collagen I-alpha2 gene expression. NRC Research Press. Can J Physiol. Pharmocol. (2015), 93: 887-892, see IDS), in view of Yu et al. (Smad4-dependent regulation of type I collagen expression in the muscle of grass carp fed with faba bean. Gene 685 (2019, Epub 10/26/2018): 32-41), Granstein et al. (Interferons and collagen production. J. Invest Dermatol. (1990), 95(6): 75S-80S, see PTO892), Duisters et al. (miR-133 and miR-30 Regulate Connective Tissue Growth Factor- Implications for a Role of MicroRNAs in Myocardial Matrix Remodeling. Circulation Research (2009), 140: 170-178, see PTO892), Aper et al. (Colorful protein based fluorescent probes for collagen imaging. PLOS ONE (2014), 9(12): e114983, p1-21, see PTO892), and Sullivan et a. (Medical devices incorporating collagen inhibitors: US 2008/0132941A1, publication 06/05/2008, see PTO892).
The Broadest Reasonable Interpretation (BRI) of claim 1, which is drawn to a method of identifying fibrotic agents capable of modulating a fibrotic process, comprising: a) contacting a plurality of immortalized or transformed fibroblasts with a test compound; b) determining a level of activity of a collagen inhibiting gene of the fibroblasts contacted with the test compound; c) comparing the level of activity of the collagen inhibiting gene to a control; and d) identifying the test compound as a fibrotic agent capable of modulating a fibrotic process when the activity of the collagen inhibiting gene indicates an upregulation or downregulation of the collagen inhibiting gene relative to the control, wherein the activity of the collagen inhibiting gene is determined by at least one of protein quantitation (amount of protein) and transcriptomic analysis (amount of mRNA transcript).
Bagchi et al. teach a method of developing of a high throughput luciferase gene system for screening activators and repressors of human collagen I-alpha2 gene expression in the context of fibrosis disease in a subject, and further teach Fibrosis, which is characterized by the excessive production of collage and matrix proteins, occurs in multiple tissues and is associated with increased morbidity and mortality despite its significant negative impact on patient outcomes, and therapies targeted to treat fibrosis are currently lacking, where, screening for inhibitors of the collagen expression, the primary component of fibrotic lesions, represents an option for the identification of novel lead compounds for therapeutic development with potentially fewer off-target effects compared with the targeting of multifunctional cell signaling pathways. Bagchi et al. also teaches generation of a stable luciferase reporter system using a fibroblast cell line, which can be used for rapidly screening both activators and repressors of human collagen COL1A2 gene transcription in a high throughput setting, and this in vitro screening tool was validated using known agonists (for increasing collagen synthesis) such as scleraxis, TGF-β, angiotensin II, CTGF, and antagonists or inhibitors (TNF-α, or pirfenidone) of COL1A2 gene expression (collagen synthesis gene), wherein where TGF-β is a collagen synthesis enhancing gene, and the TNF-α gene is a collagen inhibiting gene, and pirfenidone is a test compound which inhibit collagen synthetic gene, wherein the COL1A2-luc NIH-3T3 fibroblast system (mouse fibroblastic immortalized cell line) by using luciferase reporter gene (Luc), using eGFP (green fluorescent protein), or Renilla, a light purple or red color as reporter gene, which provides a useful and effective screen for potential lead compounds with pro- or anti-fibrotic properties (see, abstract, pg 891, left Col, para 1, and right Col, para 1), Fig. 1, and 2-4).
Claim 2 is included in this rejection because TNF-α gene encoding protein, a collagen inhibiting protein, which could be indeed druggable by tagging with any desired protein.
Bagchi et al. do not teach determining collage synthesis as 1) protein production analysis or 2) transcriptome (mRNA production) analysis, but indeed teach using luciferase for transcription analysis (for claim 1), two or more inhibitors of collagen synthesis gene from same gene family (for claim 4), test compound as siRNA, micro-RNA, or small activating RNA (for claim 5), using red fluorescent protein including mCherry, mStrawberry, mOrange, and dTomato for collagen detection (for claim 8), and treating a patient with fibrosis with a composition comprising an inhibitor of collagen synthesis through topical, injection or other administering process (for claim 11), which increase collagen synthesis (for claims 12-15, 20).
Yu et al. teach Smad4 (Collagen inhibiting gene)-dependent regulation of type I collagen expression in the muscle of grass carp fed with faba bean, and further teach that Smad4 is the key regulator in the transforming growth factor β1 (TGF-β1)/Smads signal pathway, and is also the crux of the regulation of type I collagen expression in mammals in terms of protein quantitation as amount of protein and mRNA synthesis. Given the widely accepted importance of type I collagen in fish muscle hardness, we seek to explore this issue by analyzing the expressions of the TGF-β1-Smads pathway molecules and type I collagen in the muscle of crisp grass carp fed with faba bean, which shows increased muscle hardness. The study found that (1) in the process of feeding the grass carp (fish) with faba bean, the mRNA and protein expressions of TGF-β1, Smad2 and Smad4 all increased along with the increase of type I collagen expression
(Col1α1 and Col1α2); (2) one day after the injection of Smad4 over-expression vector, both mRNA and protein expressions of Col1α1 and Col1α2 significantly increased, reaching the maximum on the 2nd and 5th day, respectively; (3) one day after the injection of Smad4 RNAi interference vector, the mRNA and protein expressions of Col1α1 and Col1α2 decreased, reaching the minimum on the 5th day, where the results revealed that Smad4 is the major regulator of type I collagen in the muscle of grass carp fed with faba bean, and interfering RNA (RNAi) of Smad4 significantly reduced collage type I synthesis. Yu et al. further teach knock-out Smad4 in the cell reduced renal fibrosis in renal tubular epithelial cell by reducing collagen synthesis, and Smad3 (see, Title, abstract, pg40, left Col 3-5, and Fig. 1-2).
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Yu et al. do not teach using two or more inhibitors that inhibit collagen synthesis (for claim 3), two or more inhibitors of collagen synthesis gene from same gene family (for claim 4), test compound as siRNA, micro-RNA, or small activating RNA (for claim 5), using red fluorescent protein including mCherry, mStrawberry, mOrange, and dTomato (for claim 8) for collagen detection, and treating a patient with fibrosis with a composition comprising an inhibitor of collagen synthesis through topical, injection or other administering process (for claim 11), which increase collagen synthesis (for claims 12-15, 20).
However, Granstein et al. teach that interferons, an immunoregulatory, antiviral and antiproliferative agent, have profound effect on collagen synthesis, specifically INF-alpha, INF-beta and INF-gamma suppresses (inhibit) collagen synthesis by human dermal fibroblast. Granstein et al. also teach that INF-gamma inhibits the constitutively increased collagen synthesis in myofibroblast and synovial fibroblast-like cells in particular type I and type III collagen synthesis by decreasing cellular mRNA of type I and type III collagen gene, where INF-alpha, INF-beta and INF-gamma are from the same gene family of interferons, a cytokine. Granstein et al. further teach synergistic effect of TNF-alpha (inhibitor of collagen synthesis)-mediated collagen synthesis inhibition (see, abstract, pg 75S, right Col, para 1-4, Table I).
Granstein et al. do not teach using test compound siRNA, micro-RNA, or small activating RNA by transcriptomic analysis of mRNA, and cDNA and followed by probe making and hybridization (for claims 5, 9, 10), using red fluorescent proteins including mCherry, mStrawberry, mOrange, and dTomato (for claim 8) for collagen detection, and treating a patient with fibrosis with a composition comprising an inhibitor of collagen synthesis through topical, injection or other administering process (for claim 11), which increase collagen synthesis (for claims 12-15, 20).
However, Duisters et al. teach micro-RNA miR-133 and miR-30 regulate connective tissue growth factor, and its implications for a role of microRNAs in myocardial matrix remodeling, and further teach that the myocardium of the failing heart undergoes a number of structural alterations, most notably hypertrophy of cardiac myocytes and an increase in extracellular matrix proteins, often seen as primary fibrosis, where connective tissue growth factor (CTGF) is a key molecule in the process of fibrosis and therefore seems an attractive therapeutic target, and regulation of CTGF expression at the promoter level, and found that CTGF transcripts are regulated at the posttranscriptional level, wherein the CTGF is importantly regulated by 2 major cardiac microRNAs (miRNAs), miR-133 and miR-30. Duisters et al. further teach that the expression of both miRNAs was inversely related to the amount of CTGF in 2 rodent models of heart disease and in human pathological left ventricular hypertrophy, where in cultured cardiomyocytes and fibroblasts, knockdown of these miRNAs increased CTGF levels, where overexpression of miR-133 or miR-30c decreased CTGF levels, which was accompanied by decreased production of collagens (see, title, abstract, Fig. 4).
Duisters et al. do not teach using red fluorescent protein including mCherry, mStrawberry, mOrange and dTomato (for claim 8) for collagen detection, and treating a patient with fibrosis with a composition comprising an inhibitor of collagen synthesis through topical, injection or other administering process (for claim 11), which increase collagen synthesis (for claims 12-15, 20).
However, Aper et al. teach colorful protein based fluorescent probes for collagen imaging using mOrange, dTomato and mCherry probe, and further teach the real-time visualization of collagen is important in studies on tissue formation and remodeling in the research fields of developmental biology and tissue engineering by using a fluorescent probe for the specific imaging of collagen in live tissue in situ, consisting of the native collagen binding protein CNA35 labeled with fluorescent dye Oregon Green 488 (CNA35-OG488), and when CNA35 is fused to fluorescent proteins that span the visible spectrum: mTurquoise2, EGFP, mOrange, dTomato and mCherry results in very visible spectrum to readout (see, abstract, Table 1, Fig. 1-2, 3-4 and 5).
Aper et al. do not teach treating a human patient with fibrosis with a composition comprising an inhibitor composition of collagen synthesis through topical (skin care), injection or other administering process (for claim 11), and increase collagen synthesis (for claims 12-15, 20).
However, Sullivan et al. teach a wound closure device comprising a composition comprising substrate and a collagen inhibitor on or in said substrate, wherein said substrate is selected from the group consisting of biodegradable substrates and non-biodegradable (inert) substrates, wherein said device is a suture, staple, tape, or bandage, wherein the substrate comprises a biodegradable polymer, poly(lactide)s, poly(glycolide)s, poly(lactide-coglycolide)s, poly(lactic acid)s, poly(glycolic acid)s, poly(lactic acid-co-glycolic acid)s, poly(caprolactone), polycarbonates, polyanhydrides, poly(amino acid)s, poly(ortho ester)s, polyamides, polyacetals, poly(ether ester)s, copolymers of poly(ethylene glycol) and poly(ortho ester)s, poly(dioxanone)s, poly(alkylene alkylate)s, biodegradable polyurethanes, and blends and copolymers thereof, wherein said substrate is a suture formed of braided, woven, or non-woven fiber material, wherein said fiber material is silk, cotton, rayon, linen, wool, satin, nylon, polyester, polypropylene, polytetrafluoroethylene or a combination thereof, wherein said collagen inhibitors are mithramycin, mitomycin-c, halofuginone and analogs thereof, and a method of treating a paranasal sinus wound in a subject in need thereof comprising topically administering a collagen inhibitor in an amount effective to treat said wound, comprising said collagen inhibitor composition (see, abstract, claims 1-14).
Therefore, it would have been obvious to one of ordinary skill in the art to arrive at the claimed invention as a whole before the effective filing date of the invention was made by combining the teachings of Bagchi et al., Yu et al., Granstein et al., Duisters et al., Aper et al. and Sullivan et al. for detection and analysis of transcription modulation by protein production analysis or transcriptome analysis as taught by Yu et al., using two or more inhibitors that inhibit collagen synthesis as taught by Bagchi et al., using two or more inhibitors of collagen synthesis gene from same gene family as taught by Granstein et al., using test compounds, which are siRNA, micro-RNA, or small activating RNA as taught by Duisters et al., using red fluorescent protein including mCherry, mStrawberry, mOrange and dTomato for collagen detection as taught by Aper et al., treating a patient with collagen inhibiting compositions of a patient, and modify Bagchi et al. in view of the teachings of Yu et al. Granstein et al., Duisters et al., Aper et al. and Sullivan to reduce collagen synthesis for treating fibrosis to arrive the claimed invention.
One of ordinary skilled in the art would have been motivated to use test compound, which inhibit collagen synthesis for treating fibrosis in a patient which is therapeutically, clinically, pharmaceutically and financially beneficial.
One of ordinary skilled in the art would have a reasonable expectation of success because Bagchi et al. teach a method of developing of a high throughput luciferase gene system for screening activators and repressors of human collagen I-alpha2 gene expression in the context of fibrosis disease in a subject, and Sullivan could successfully treat human patient with fibrotic disorder using collagen inhibitors.. Thus, the above references render the claims prima facie obvious to one of ordinary skill in the art.
Conclusion
Status of the claims:
Claims 1-2, 3-5, 7, 8-15, 16, 17-19 and 20 are rejected.
Applicant's amendments (see, substantial amendments of claim 1), necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action. Any inquiry concerning this communication or earlier communications from the examiner should be directed to IQBAL H CHOWDHURY whose telephone number is (571)272-8137. The examiner can normally be reached on M-F, at 9:00-5:00 PM.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao, can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
Iqbal H. Chowdhury, PhD.
Primary Patent Examiner
Art Unit 1656 (Recombinant Enzymes and Protein Crystallography)
US Patent and Trademark Office (USPTO)
Ph. (571)-272-8137 and Fax (571)-273-8137
/IQBAL H CHOWDHURY/
Primary Examiner, Art Unit 1656