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K Lindblom

Publications and source records attributed to K Lindblom.

5 recordsLinked to original sources
PubMed1992

COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins.

Cloning and sequence analysis of cartilage oligomeric matrix protein (COMP) cDNA, representing a cartilage pentameric protein, revealed a protein of 755 amino acid residues with a calculated molecular mass of 82,700 Da. Expression of the cDNA in COS cells showed that COMP is a homopolymer composed of five identical disulfide-linked subunits. COMP is homologous to the carboxyl-terminal half of thrombospondin, and the homologies include 89% and 54% of the residues in COMP and thrombospondin, respectively. The similarities are most pronounced in the carboxyl-terminal domains and in the calcium binding type 3 repeat domains in which about 60% of the amino acid residues are identical. In the type 2/epidermal growth factor repeat domains the two proteins contain 41% identical residues. The sequence of the amino-terminal 84-amino acid residues is unique for COMP. Comparison of the amino acid sequences in the type 2 and type 3 repeat domains of COMP and the thrombospondins shows that COMP is the product of a unique gene and not the result of an alternatively spliced thrombospondin gene.

Amino Acid Sequence↗
PubMed1989

A collagen-binding 59-kd protein (fibromodulin) is structurally related to the small interstitial proteoglycans PG-S1 and PG-S2 (decorin).

We have determined the primary structure of a 59 kd collagen binding protein which is present in many types of connective tissues, e.g. cartilage, tendon, skin, sclera and cornea. The amino acid sequence, deducted from a 2662 bp cDNA clone, predicts a 42 kd protein with a high content of leucine residues. Most of the protein consists of homologous 23 amino acid residues repeats with predominantly leucine residues in conserved positions. Similar leucine rich repeats have been identified in a number of proteins including the small interstitial proteoglycans decorin and PG-S1. The 59 kd protein and the two proteoglycans are homologous in their entire sequences suggesting that they have evolved from a common ancestral gene. The 59 kd protein and decorin are also functionally related in that both bind to collagen type I and II, and affect their fibrillogenesis. The substitution with glycosaminoglycan chains appears to be a feature shared by all three members of this family of leucine rich motif extracellular proteins, since the 59 kd protein isolated from cartilage is substituted with at least one keratan sulfate chain.

Amino Acid Sequence↗
PubMed1988

Induction of single-strand breaks in liver DNA of mice after inhalation of vinyl chloride.

NMRI female mice were exposed to 100, 250 and 500 ppm vinyl chloride (VC). Cell nuclei were prepared from the liver, and single-strand breaks (SSB) were determined by the DNA unwinding technique. Haemoglobin (Hb) was isolated from the blood, and the degree of alkylation was determined as a measure of in-vivo dose by means of a gas chromatography-mass spectrometry (GC-MS) technique. A maximum level of SSB in liver DNA and of adduct levels of Hb was reached at 500 ppm, indicating that saturation of metabolic activation of VC had been achieved. The results demonstrate that VC induces SSB in liver DNA of mice in a dose-dependent manner and that about 80% of the damage is repaired within 20 h.

Administration, Inhalation↗