Identification of cDNA clones encoding different domains of the basement membrane heparan sulfate proteoglycan

D. M. Noonan, E. A. Horigan, S. R. Ledbetter, G. Bogeli, M. Sasaki, Y. Yamada, J. R. Hassell

Research output: Contribution to journalArticlepeer-review

Abstract

We have used antibodies to the basement membrane proteoglycan to screen λgt11 expression vector libraries and have isolated two cDNA clones, termed BPG 5 and BPG 7, which encode different portions of the core protein of the heparan sulfate basement membrane proteoglycan. These clones hybridize to a single mRNA species of approximately 12 kilobases. Amino acid sequences obtained on peptides derived from protease digests of the core protein were found in the deduced sequence, confirming the identity of these clones. BPG 5 spanned 1986 base pairs and has an open reading frame of 662 amino acids. The amino acids sequence deduced from BPG 5 contains two cysteine-rich domains and two internally homologous domains lacking cysteine. The cysteine-rich domains show homology to the cysteine-rich domains of the laminin chains. A globule-rod structure, similar to that of the short arms of the laminin chains, is proposed for this region of the proteoglycan. The other clone, BPG 7, is 2193 base pairs long and has an open reading frame of 731 amino acids. The deduced sequence contains eight internal repeats with 2 cysteine residues in each repeat. These repeats show homology to the neural-cell adhesion molecule N-CAM and the plasma α1B-glycoprotein. Looping structures similar to these proteins and to other proteins of the immunoglobulin gene superfamily are proposed for this region of the proteoglycan. The sequency DSGEY was found four times in this domain and could be heparan sulfate attachment sites.

Original languageEnglish
Pages (from-to)16379-16387
Number of pages9
JournalJournal of Biological Chemistry
Volume263
Issue number31
Publication statusPublished - 1988

ASJC Scopus subject areas

  • Biochemistry

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