Alkaline phosphatase binds to collagen; a hypothesis on the mechanism of extravesicular mineralization in epiphyseal cartilage

Vittur, Franco; Stagni, N.; Moro, Luigi; Bernard, B. de

doi:10.1007/bf01951980

Cited by 54 publications

(21 citation statements)

References 18 publications

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“…Initial experiments using affinity chromatography, identified collagen type I, II, and X as binding partners of TNAP [573][574][575]. The interaction of collagens with TNAP is thought to be important as a nucleator for the process of skeletal calcification.…”

Section: Protein Interactionsmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

871

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: Protein Interactionsmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

871

922

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“…The mechanism by which MV-initiated HA crystals transfer to collagen fibers remains elusive. However, some previous results suggest the formation of a collagen-ALP complex as a step in the process initiating the deposit of crystalline HA in and around collagen fibrils [63,64] (Fig. 3).…”

Section: Mineralization Of Bone Matrixmentioning

confidence: 89%

“…Prior studies have mainly reported binding of various ALP isozymes to collagen type II [58,63,64,102]. In paper III, we investigated the binding properties of human BALP to human collagen type I, the major structural component in the extracellular matrix of bone.…”

Section: Paper IIImentioning

confidence: 99%

Biochemical and functional properties of mammalian bone alkaline phosphatase isoforms during osteogenesis

Linder

2016

Linköping University Medical Dissertations

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The human skeleton is a living and dynamic tissue that constantly is being renewed in a process called bone remodeling. Old bone is resorbed by osteoclasts and new bone is formed by osteoblasts. Bone is a composite material made up by mineral crystals in the form of hydroxyapatite (calcium and phosphate) that provides the hardness of bone, and collagen fibrils that provides elasticity and flexibility. Alkaline phosphatase (ALP) is a family of enzymes that is present in most species and catalyzes the hydrolysis of various phosphomonoesters at alkaline pH. Despite the generalized use of ALP as a biochemical marker of bone formation, the precise function of bone ALP (BALP) is only now becoming clear. Three circulating human BALP isoforms (B1, B2, and B/I) can be distinguished in healthy individuals and a fourth isoform (B1x) has been discovered in patients with chronic kidney disease and in bone tissue.Paper I. Three endogenous phosphocompounds, (i.e., inorganic pyrophosphate (PPi), pyridoxal 5′-phosphate (PLP) and phosphoethanolamine (PEA)), have been suggested to serve as physiological substrates for BALP. The BALP isoforms display different catalytic properties towards PPi and PLP, which is attributed to their distinct N-linked glycosylation patterns. The catalytic activity, using PEA as substrate, was barely detectable for all BALP isoforms indicating that PEA is not a physiological substrate for BALP.Paper II. Mouse serum ALP is frequently measured and interpreted in mammalian bone research. However, little is known about the circulating ALPs in mice and their relation to human ALP. We characterized the circulating and tissue-derived mouse ALP isozymes and isoforms from mixed strains of wild-type and knockout mice. All four BALP isoforms (B/I, B1x, B1, and B2) were identified in mouse serum and bone tissues, in good correspondence with those found in human bones. All mouse tissues, except liver, contained significant ALP activities. This is a notable difference as human liver contains vast amounts of ALP.Paper III. The objective of this study was to investigate the binding properties of human collagen type I to human BALP, including the two BALP isoforms B1 and B2, together with ALP from human liver, human placenta and E. coli. A surface plasmon resonance-based analysis showed that BALP binds stronger to collagen type I in comparison with ALPs expressed in non-mineralizing tissues. The B2 isoform binds significantly stronger to collagen IV type I in comparison with the B1 isoform, indicating that glycosylation differences in human ALPs are of crucial importance for protein-protein interactions with collagen type I.Paper IV. Tartrate-resistant acid phosphatase (TRAP) is highly expressed in osteoclasts and frequently used as a marker of bone resorption. Intriguingly, recent studies show that TRAP is also expressed in osteoblasts and osteocytes. TRAP displays enzymatic activity towards the endogenous substrates for BALP, i.e., PPi and PLP. Both TRAP and BALP can alleviate the inhibitory effect of osteopon...

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“…Chicken TNAP is known to bind collagen I, 11, and X (Vittur et al, 1984;Wu et al, 19911, a property which has been attributed in part to a flexible surface loop in the region between K405 and V442 of mTNAP (Bossi et al, 1993). Although the mammalian enzymes are almost identical in this region, chTNAP shows only 76.4% conservation.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to its enzymatic activity, it has been suggested that AP might function as a structural cell surface molecule capable of directing cell migration and adhesion in development Steinberg, 1988, 1989). In support of a structural role for AP is the demonstration that AP can bind to collagen (Vittur et al, 1984;Wu et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Tissue‐nonspecific alkaline phosphatase participates in the establishment and growth of feather germs in embryonic chick skin cultures

Crawford

Weissig

Binette

et al. 1995

Developmental Dynamics

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Alkaline phosphatase activity is present in the mesoderm of embryonic chick skin and becomes spatially restricted to the dermal condensation of the developing feather germs. Inhibitors to tissue-nonspecific (liver/bone/kidney), but not intestinal, alkaline phosphatase inhibit the establishment and growth of feather germs in cultured skins. A window of maximum sensitivity to the inhibitor was observed to be the first day of culture when early development and establishment of pattern takes place. The cDNA for the avian tissue-nonspecific alkaline phosphatase was cloned and sequenced, and Southern analysis revealed a single copy of this gene in the avian genome. Northern analysis revealed that a 2.8 kb transcript for this form of alkaline phosphatase is present in developing skin. o 1995 Wiley-Liss, Inc.

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Alkaline phosphatase binds to collagen; a hypothesis on the mechanism of extravesicular mineralization in epiphyseal cartilage

Cited by 54 publications

References 18 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Biochemical and functional properties of mammalian bone alkaline phosphatase isoforms during osteogenesis

Tissue‐nonspecific alkaline phosphatase participates in the establishment and growth of feather germs in embryonic chick skin cultures

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