Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain

M. Warman, T. Kimura, Y. Muragaki, P. Castagnola, H. Tamei, K. Iwata, B. R. Olsen

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Type IX collagen is a component of cartilage and vitreous humor. Its structure and matrix localization suggest it may serve to mediate interactions between fibrillar collagen, proteoglycan and other matrix components. Consequently, abnormalities in type IX collagen may result in chondrodysplasia. In this paper we describe the preparation and use of two monoclonal antibodies which recognize peptide sequences within the human cartilage α1(IX) collagen chain. Antibody 23-5D1 is highly sensitive and highly specific. It permits the immunoblot detection of type IX collagen extracted from milligram amounts of normal and chondrodysplastic cartilage; it also identifies the 'short' form of the α1(IX) chain in human vitreous humor. Antibody 37 10H7 is highly specific, but of low sensitivity. It was used to make the new observation that an N-linked oligosaccharide is present in the amino-terminal globular domain of the α1 (IX) chain. We anticipate that these antibodies may be valuable tools in the study of human and other mammalian chondrodysplasias.

Original languageEnglish
Pages (from-to)149-156
Number of pages8
JournalMatrix
Volume13
Issue number2
Publication statusPublished - 1993

Fingerprint

Collagen Type IX
Enchondromatosis
Cartilage
Epitopes
Vitreous Body
Collagen
Monoclonal Antibodies
Antibodies
Fibrillar Collagens
Proteoglycans
Oligosaccharides
Peptides

Keywords

  • Antibodies
  • Type IX collagen

ASJC Scopus subject areas

  • Rheumatology

Cite this

Warman, M., Kimura, T., Muragaki, Y., Castagnola, P., Tamei, H., Iwata, K., & Olsen, B. R. (1993). Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain. Matrix, 13(2), 149-156.

Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain. / Warman, M.; Kimura, T.; Muragaki, Y.; Castagnola, P.; Tamei, H.; Iwata, K.; Olsen, B. R.

In: Matrix, Vol. 13, No. 2, 1993, p. 149-156.

Research output: Contribution to journalArticle

Warman, M, Kimura, T, Muragaki, Y, Castagnola, P, Tamei, H, Iwata, K & Olsen, BR 1993, 'Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain', Matrix, vol. 13, no. 2, pp. 149-156.
Warman M, Kimura T, Muragaki Y, Castagnola P, Tamei H, Iwata K et al. Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain. Matrix. 1993;13(2):149-156.
Warman, M. ; Kimura, T. ; Muragaki, Y. ; Castagnola, P. ; Tamei, H. ; Iwata, K. ; Olsen, B. R. / Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain. In: Matrix. 1993 ; Vol. 13, No. 2. pp. 149-156.
@article{7a11b448d97244dfa09e1f194e81b00b,
title = "Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain",
abstract = "Type IX collagen is a component of cartilage and vitreous humor. Its structure and matrix localization suggest it may serve to mediate interactions between fibrillar collagen, proteoglycan and other matrix components. Consequently, abnormalities in type IX collagen may result in chondrodysplasia. In this paper we describe the preparation and use of two monoclonal antibodies which recognize peptide sequences within the human cartilage α1(IX) collagen chain. Antibody 23-5D1 is highly sensitive and highly specific. It permits the immunoblot detection of type IX collagen extracted from milligram amounts of normal and chondrodysplastic cartilage; it also identifies the 'short' form of the α1(IX) chain in human vitreous humor. Antibody 37 10H7 is highly specific, but of low sensitivity. It was used to make the new observation that an N-linked oligosaccharide is present in the amino-terminal globular domain of the α1 (IX) chain. We anticipate that these antibodies may be valuable tools in the study of human and other mammalian chondrodysplasias.",
keywords = "Antibodies, Type IX collagen",
author = "M. Warman and T. Kimura and Y. Muragaki and P. Castagnola and H. Tamei and K. Iwata and Olsen, {B. R.}",
year = "1993",
language = "English",
volume = "13",
pages = "149--156",
journal = "Matrix",
issn = "0934-8832",
publisher = "Fischer Medical Publications",
number = "2",

}

TY - JOUR

T1 - Monoclonal antibodies against two epitopes in the human α1(IX) collagen chain

AU - Warman, M.

AU - Kimura, T.

AU - Muragaki, Y.

AU - Castagnola, P.

AU - Tamei, H.

AU - Iwata, K.

AU - Olsen, B. R.

PY - 1993

Y1 - 1993

N2 - Type IX collagen is a component of cartilage and vitreous humor. Its structure and matrix localization suggest it may serve to mediate interactions between fibrillar collagen, proteoglycan and other matrix components. Consequently, abnormalities in type IX collagen may result in chondrodysplasia. In this paper we describe the preparation and use of two monoclonal antibodies which recognize peptide sequences within the human cartilage α1(IX) collagen chain. Antibody 23-5D1 is highly sensitive and highly specific. It permits the immunoblot detection of type IX collagen extracted from milligram amounts of normal and chondrodysplastic cartilage; it also identifies the 'short' form of the α1(IX) chain in human vitreous humor. Antibody 37 10H7 is highly specific, but of low sensitivity. It was used to make the new observation that an N-linked oligosaccharide is present in the amino-terminal globular domain of the α1 (IX) chain. We anticipate that these antibodies may be valuable tools in the study of human and other mammalian chondrodysplasias.

AB - Type IX collagen is a component of cartilage and vitreous humor. Its structure and matrix localization suggest it may serve to mediate interactions between fibrillar collagen, proteoglycan and other matrix components. Consequently, abnormalities in type IX collagen may result in chondrodysplasia. In this paper we describe the preparation and use of two monoclonal antibodies which recognize peptide sequences within the human cartilage α1(IX) collagen chain. Antibody 23-5D1 is highly sensitive and highly specific. It permits the immunoblot detection of type IX collagen extracted from milligram amounts of normal and chondrodysplastic cartilage; it also identifies the 'short' form of the α1(IX) chain in human vitreous humor. Antibody 37 10H7 is highly specific, but of low sensitivity. It was used to make the new observation that an N-linked oligosaccharide is present in the amino-terminal globular domain of the α1 (IX) chain. We anticipate that these antibodies may be valuable tools in the study of human and other mammalian chondrodysplasias.

KW - Antibodies

KW - Type IX collagen

UR - http://www.scopus.com/inward/record.url?scp=0027516785&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027516785&partnerID=8YFLogxK

M3 - Article

VL - 13

SP - 149

EP - 156

JO - Matrix

JF - Matrix

SN - 0934-8832

IS - 2

ER -