1986•Proceedings annual meeting Electron Microscopy Society of AmericaRequires access

C-propeptide of type ii procollagen; a protein associated with cartilage mineralization

E.R. Lee, A. Robin Poole

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Abstract

A matrix protein has been identified in both calcifying and noncalcifying cartilage during development, and named chondrocalcin. The concentration of this protein is greatly increased in calcifying cartilage and it appears in the matrix when and where mineralization occurs. Amino acid sequencing has recently shown that chondrocalcin is identical to the C-propeptide of type II procollagen. Type II procollagen is a high molecular weight precursor of type II collagen and it is characterized by amino (NH2) and carboxy (C) propeptide extensions. These nonhelical extensions are normally cleaved extracellularly by proteinases to give the collagen molecule. To investigate the synthesis, secretion and matrix distribution of the C-propeptide, particularly during mineralization, this protein has been localized at the EM level with immunogold techniques.

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What this paper is about

A matrix protein has been identified in both calcifying and noncalcifying cartilage during development, and named chondrocalcin. The concentration of this protein is greatly increased in calcifying cartilage and it appears in the matrix when and where mineralization occurs. Amino acid sequencing has recently shown that chondrocalcin is identical to the C-propeptide of type II procollagen. Type II procollagen is a high molecular weight precursor of type II collagen and it is characterized by amino (NH2) and carboxy (C) propeptide extensions. These nonhelical extensions are normally cleaved extracellularly by proteinases to give the collagen molecule. To investigate the synthesis, secretion and matrix distribution of the C-propeptide, particularly during mineralization, this protein has been localized at the EM level with immunogold techniques.

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Available abstract

A matrix protein has been identified in both calcifying and noncalcifying cartilage during development, and named chondrocalcin. The concentration of this protein is greatly increased in calcifying cartilage and it appears in the matrix when and where mineralization occurs. Amino acid sequencing has recently shown that chondrocalcin is identical to the C-propeptide of type II procollagen. Type II procollagen is a high molecular weight precursor of type II collagen and it is characterized by amino (NH2) and carboxy (C) propeptide extensions. These nonhelical extensions are normally cleaved extracellularly by proteinases to give the collagen molecule. To investigate the synthesis, secretion and matrix distribution of the C-propeptide, particularly during mineralization, this protein has been localized at the EM level with immunogold techniques.

Key concepts: Procollagen peptidase, Protein precursor, Cartilage, Immunogold labelling, Mineralization (soil science), Chemistry, Extracellular matrix, Secretion

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