The interaction of a component of bone organic matrix with the mineral phase

Wilson, J. M.; Ashton, Brian A.; Triffitt, James T.

doi:10.1007/bf02064129

Cited by 20 publications

(11 citation statements)

References 3 publications

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“…The concentration of AHSG progressively falls in bone throughout childhood to adult life (8); fetal bone was reported to contain at least 10 times more AHSG than does adult bone (9), while neonatal bone contains 7 times more AHSG than does adult bone (10).…”

mentioning

confidence: 99%

Human alpha 2-HS-glycoprotein: the A and B chains with a connecting sequence are encoded by a single mRNA transcript.

Lee¹,

Bowman²,

Yang³

1987

Proc. Natl. Acad. Sci. U.S.A.

100

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The a2-HS-glycoprotein (AHSG) is a plasma protein reported to play roles in bone mineralization and in the immune response. It is composed of two subunits, the A and B chains. Recombinant plasmids containing human cDNA AHSG have been isolated by screening an adult human liver library with a mixed oligonucleotide probe. The cDNA clones containing AHSG inserts span approximately 1.5 kiobase pairs and include the entire AHSG coding sequence, demonstrating that the A and B chains are encoded by a single mRNA transcript. The cDNA sequence predicts an 18-amino-acid signal peptide, followed by the A-chain sequence of AHSG. A heretofore unseen connecting sequence of 40 amino acids was deduced between the A-and B-chain sequences. The connecting sequence demonstrates the unique amino acid doublets and collagen triplets found in the A and B chains; it is not homologous with other reported amino acid sequences. The connecting sequence may be cleaved in a posttranslational step by limited proteolysis before mature AHSG is released into the circulation or may vary in its presence because of alternative processing. The AHSG cDNA was utilized for mapping the AHSG gene to the 3q21-*qter region of human chromosome 3. The availability of the AHSG cDNA clone will facilitate the analysis of its genetic control and gene expression during development and bone formation.The human a2-HS-glycoprotein (AHSG) is a plasma protein that consists of two subunits, an A chain of 282 amino acids and a B chain of 27 amino acids (1, 2). The A chain and B chain are linked through a disulfide bond. The molecule has interesting and unique features; there are 29 amino acid doublets in circulating AHSG with Ala-Ala or Ala-Ala-Ala

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mentioning

confidence: 99%

Human alpha 2-HS-glycoprotein: the A and B chains with a connecting sequence are encoded by a single mRNA transcript.

Lee¹,

Bowman²,

Yang³

1987

Proc. Natl. Acad. Sci. U.S.A.

100

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“…Adult human bone and foetal calvaria contain 0.25 and 3.8 mg of qHS-glycoprotein/g of dry tissue respectively (Wilson, Ashton & Triffitt, 1977) and the qHSglycoprotein content of bone formed in Paget's disease would be expected to be between these two values (say 1 mg/g). Kinetic analysis with "Ca suggests that the depositional rate for calcium in patients with Paget's disease varies considerably, with values of 2.5-14.5 g/day found by Nagant de Deuxchaisnes & Krane (1964); these are equivalent to a bone formation rate of 6-38 g daily, compared…”

Section: Discussionmentioning

confidence: 99%

Plasma α2 HS-glycoprotein Concentration in Paget's Disease of Bone: its Possible Significance

Ashton

Smith

1980

Clinical Science

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1. The plasma concentration of the alpha 2HS-glycoprotein has been measured in 58 normal adults and in patients with Paget's disease of bone before (24) and during treatment (16). 2. The average plasma alpha 2HS-glycoprotein was lower in the patients with Paget's disease than in the normal adults and was inversely related to plasma alkaline phosphatase activity (r = -0.55, n = 24, P less than 0.001). 3. When the patients with Paget's disease were treated with either diphosphonate or calcitonin, the plasma alpha 2HS-glycoprotein concentration increased towards normal. In those patients treated with calcitonin, this increase was too rapid to be entirely accounted for by a cessation of bone formation.

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“…It is well known that bone mineralisation is related to non-collagenous proteins of bone matrix and that albumin coming from plasma is one of these proteins. [15][16][17][18][19][20][21][22] In addition, albumin reduces the phagocytic recognition of bone mineral by macrophages. 23 By contrast, the low albumin concentration in aged people and lower concentration in patients with femoral neck fractures (even though in both cases the values were non-significant) suggests the possibility of the opposite nutritional condition in such subjects.…”

Section: Conceptual Implicationsmentioning

confidence: 99%

Raised serum albumin in hip osteoarthrosis: a comparative study in women of some blood chemical parameters in aging and in cases of femoral neck fractures, osteoporotic vertebral crush fractures, and hip osteoarthrosis.

Rapin¹,

Lagier²

1988

Annals of the Rheumatic Diseases

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The interaction of a component of bone organic matrix with the mineral phase

Cited by 20 publications

References 3 publications

Human alpha 2-HS-glycoprotein: the A and B chains with a connecting sequence are encoded by a single mRNA transcript.

Human alpha 2-HS-glycoprotein: the A and B chains with a connecting sequence are encoded by a single mRNA transcript.

Plasma α2 HS-glycoprotein Concentration in Paget's Disease of Bone: its Possible Significance

Raised serum albumin in hip osteoarthrosis: a comparative study in women of some blood chemical parameters in aging and in cases of femoral neck fractures, osteoporotic vertebral crush fractures, and hip osteoarthrosis.

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