Abstract: An enzyme linked immunosorbent assay (ELISA) kit for the quantification of degradation products of carboxy-terminal telopeptides of type I collagen in a human serum sample, including an antibody that is characterized by binding to at least one peptide derived from the carboxy-terminal telopeptide domain of type I collagen and isolatable from a urine sample of a patient with active Paget's disease.
Abstract: A composition or device suitable for orthopedic or dental implantation to bone, characterized by tartrate-resistant acid phosphatase (TRAP) adsorbed to a porous hydroxyapatite substratum.
Type:
Grant
Filed:
April 21, 1998
Date of Patent:
February 20, 2001
Assignee:
Washington Research Foundation
Inventors:
Minako Yoshioka Lee, David Rodney Eyre, Mary Ann Eklof Weis
Abstract: Immunoassay test kit for detecting analyte indicative of type II collagen resorption in vivo. including an immunological binding partner which binds to an amino-terminal or carboxy-terminal 3-hydroxypyridinium cross-linked telopeptide of type II collagen isolatable from a urine sample of a growing adolescent. Preferably the immunological binding partner does not cross-react more than 10% with the type I and type III collagen telopeptides of formulas III, VI, VIII, X, IX, and XI.
Abstract: An intraocular lens is described that includes an optic portion formed of an optically suitable polymer or glass material that has been coated by a fluorocarbon polymer. A haptic portion of the IOL is attached to the optic. The resulting low-energy IOL surface induces significantly reduced cell damage when contacted with corneal endothelial tissues. The fluorocarbon polymer coating is preferably applied by exposing IOL surfaces to a plasma formed from a gaseous fluorocarbon monomer. The resulting IOL causes substantially less damage to corneal endothelial cells during implantation.
Abstract: Sandwich immunoassays for detecting analyte indicative of type II collagen resorption in vivo, by contacting a body fluid sample with a first antibody and a second antibody such that analyte present in the sample forms a first antibody-analyte-second antibody complex, and detecting the presence or amount of the first antibody-analyte-second antibody complex, wherein the first and second antibodies are capable of binding to a telopeptide having a sequence identical to that of a carboxy-terminal telopeptide produced in vivo upon degradation of type II collagen.
Abstract: Peptides synthesized to match the human .alpha.1(II) carboxy-telopeptide sequences of type II collagen degradation products in body fluids, preferably Glu-Lys-Gly-Pro-Asp-Pro (SEQ ID NO:6). Useful as calibrators and antigens in immunoassays for detecting type II collagen degradation products in body fluids.
Abstract: Sandwich immunoassays for detecting analyte indicative of type 1 collagen resorption in vivo, by contacting a body fluid sample with a first antibody and a second antibody such that analyte present in the sample forms a first antibody-analyte-second antibody complex, and detecting the presence or amount of the first antibody-analyte-second antibody complex, wherein the first and second antibodies are capable of binding to a telopeptide having a sequence identical to that of an amino-terminal or carboxy-terminal telopeptide produced in vivo upon degradation of type 1 collagen are claimed.
Abstract: A system for detecting Barrett's metaplasia utilizes an illumination and imaging probe at the end of a catheter. The probe illuminates the wall of the esophagus and returns reflected light to be processed to provide a visual indication of the color of the esophageal wall. The position of the probe along the length of the esophagus is also measured to allow a medical practitioner to determine the location of the transition from the pink stomach lining to the white esophageal lining.
Type:
Grant
Filed:
June 17, 1997
Date of Patent:
March 7, 2000
Assignee:
Washington Research Foundation
Inventors:
Fred E. Silverstein, Roy W. Martin, Darik Taniguchi, John A. Myers
Abstract: Methods and compositions are provided for the production of a polypeptide which is immunologically cross-reactive with a naturally-occurring major outer membrane protein (MOMP) of Chlamydia trachomatis. A DNA construct including a replication system recognized by E. coli, and an MOMP gene under the transcriptional control of a .beta.-glactosidase promoter and terminator is provided. Recombinant phage .lambda.gtll/L2/33 was deposited at the American Type Culture Collection, 12301 Parklawn Drive, Rockville, Md. 20852, on Jan. 10, 1985 and granted accession no. 40157. L2 B9-F DNA was deposited at the American Type Culture Collection on Dec. 31, 1985, and granted accession No. 40217.
Type:
Grant
Filed:
June 6, 1995
Date of Patent:
February 29, 2000
Assignee:
Washington Research Foundation
Inventors:
Nina Agabian, Richard Stephens, Cho-Chou Kuo, Guy Mullenbach
Abstract: Immunoassay test kit for detecting analyte indicative of type I collagen resorption in vivo, comprising an immunological binding partner which binds to an amino-terminal or carboxy-terminal 3-hydroxypyridinium cross-linked telopeptide of type I collagen isolatable from a urine sample of a patient with active Paget's disease, wherein the immunological binding partner does not cross-react more than 10% with the type II and type III collagen telopeptides of formulas XVI, XIV, XII, XI, VII, VIII, X, IX, and XI.
Abstract: DNA sequences to mammalian .alpha..sub.1 -antitrypsin are provided which can be used for expression of mammalian .alpha..sub.1 -antitrypsin.This work was supported in part by grants HL16919 and HL27509 from the National Institutes of Health.
Type:
Grant
Filed:
January 20, 1998
Date of Patent:
February 15, 2000
Assignee:
Washington Research Foundation
Inventors:
Earl W. Davie, Kotoku Kurachi, Savio L. C. Woo, Chandra Thirumalachary
Abstract: An immunoassay test kit including an immunological binding partner that binds to lysyl pyridinoline, for analyzing a body fluid sample for bone resorption in vivo.
Abstract: In a method of analyzing a body fluid sample for the presence of analyte indicative of a physiological condition, comprising the steps of contacting the body fluid sample with an immunological binding partner which binds to the analyte, detecting binding of the immunological binding partner to the analyte, and correlating any detected binding to the physiological condition, the improvement comprising contacting the body fluid sample with an immunological binding partner which binds to(Gln)-(Tyr)-(Ser)-(Tyr)-(Asp)-(Val)-Hyl- .vertline. (Gln)-(Tyr)-(Ser)-(Tyr)-(Asp)-(Val)-Hyl- .vertline. (Gly)-Ile-Hyl- -Ser-Gly-Val-Ala-Val-Gly-Gly -Ser-Gly-Val-Ala-Val-Gly-Gly -Gly-His-Argwherein the cross-linking residue depicted as Hyl-Hyl-Hyl is hydroxylysyl pyridinoline and the parentheses indicate optional amino acid residues, and correlating any detected binding to degradation of type III collagen in vivo.
Abstract: Urinary assay for measuring bone resorption, by contacting an unhydrolyzed urine sample with an antibody that binds to free lysyl pyridinoline cross-links, detecting any binding of the antibody in the body fluid sample, and correlating the detected binding to bone resorption in vivo. The free lysyl pyridinoline cross-links are preferably measured as a ratio to the creatinine content in order to provide a urinary index of bone resorption independent of urine volume.
Abstract: Peptides synthesized to match the human .alpha.1(I) and .alpha.2(I) telopeptide sequences of the type I collagen metabolites, preferably selected from among Asp-Glu-Lys-Ser-Thr-Gly-Gly (SEQ ID NO:5), Gln-Tyr-Asp-Gly-Lys-Gly-Val-Gly (SEQ ID NO:6), and Glu-Lys-Ala-His-Asp-Gly-Gly-Arg (SEQ ID NO:7). Useful as calibrators and antigens in immunoassays for detecting type I collagen degradation products in body fluids.
Abstract: A method for assaying bone resorption rates which consists of quantitating the concentration of free lysyl pyridinoline derived from bone collagen, found in a body fluid is disclosed. The method includes immunometric assay, fluorometric assay and electrochemical titration. The structure of specific 3-hydroxypyridinium cross-links found in urine of Paget's disease patients and procedures for making monoclonal antibodies is described.
Abstract: Method of monitoring a patient's response to an anti-resorptive therapy such as estrogen, by contacting a body fluid sample of the patient with an immunological binding partner specific for a cross-linked telopeptide having a sequence identical to that of a cross-linked amino-terminal or carboxy-terminal telopeptide produced in vivo upon degradation of type I collagen, detecting any binding of the immunological binding partner in the body fluid sample, and correlating the detected binding to the rate of bone resorption in the patient.
Abstract: In a method of analyzing a body fluid sample for the presence of an analyte indicative of a physiological condition, comprising the steps of contacting the body fluid sample with an immunological binding partner which binds to the analyte, detecting binding of the immunological binding partner to the analyte, and correlating any detected binding to the physiological condition, the improvement comprising contacting the body fluid sample with an immunological binding partner which binds to ##STR1## wherein ##STR2## is hydroxylysyl pyridinoline or lysyl pyridinoline, and correlating any detected binding to degradation of type II collagen in vivo.
Abstract: DNA expression vectors capable, in a transformant strain of yeast, of expressing a polypeptide under the control of a genetically distinct yeast promoter, processes of forming transformant strains of yeast and transformed yeast strains are disclosed.
Type:
Grant
Filed:
June 6, 1995
Date of Patent:
July 6, 1999
Assignees:
Washington Research Foundation, Genentech, Inc.
Inventors:
Ronald A. Hitzeman, Franklin E. Hagie, IV, Benjamin D. Hall, Gustav Ammerer
Abstract: Compositions useful in quantitating collagen peptides to determine the rate of bone resorption are prepared by treating bone with a protease, such as collagenase, and purifying the compositions so as to enrich them with peptides that contain 3-hydroxypyridinium cross-links.