Title : Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA
Abstract :
- The core protein of a small chondroitin/dermatan sulfate proteoglycan expressed by human fibroblasts and present in extracellular matrices in association with collagen has been cloned from a lambda gt11 fibroblast cDNA library
- cDNA clones were isolated by use of antibodies specific for the intact proteoglycan and antibodies against a peptide synthesized on the basis of the amino-terminal sequence of the core protein
- A 1.8-kilobase cDNA was found to code for a prepro core protein composed of a signal peptide , a propeptide , and a mature core protein of 329 amino acids
- The amino-terminal amino acid sequence deduced from the cDNA sequence was identical to that previously obtained by protein sequencing
- The core protein contains three Ser-Gly dipeptide sequences , of which one is substituted with glycosaminoglycan
- A protein data base homology search established the core protein sequence is a unique sequence distinct from published amino acid sequences
- RNA blot hybridizations, performed using the cloned cDNA as a probe, revealed two related transcripts of 1.6 and 1.9 kilobases in RNA from both human fibroblast and placental tissue
- Hybridization of genomic DNA restriction fragments suggested that there is one gene for the core protein of this proteoglycan and possibly one other closely related gene
- Availability of the cloned cDNA for the proteoglycan now makes it possible to apply methods of molecular biology to study the collagen-binding and cell attachment-inhibiting properties of this proteoglycan
Output (sent_index, trigger,
protein,
sugar,
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Output(Part-Of) (sent_index,
protein,
site):
- 2. protein, sequence
- 5. protein, sequences
- 6. protein, sequence
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):