Structural comparison of the 68 kDa laminin-binding protein and 5′-nucleotidase from chicken muscular sources: Evidence against a gross structural similarity of both proteins

Risse, G; Stochaj, Ursula; Elsässer, Katharina; Dieckhoff, J; Mannherz, Hans Georg; Mark, Klaus von der

doi:10.1016/0167-4838(89)90302-6

Cited by 7 publications

(3 citation statements)

References 16 publications

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“…Subsequent sequencing has identified some of these proteins as 5'-nucleotidase (Misumi et al, 1990), aspartactin (Clegg et al, 1989), and a splice variant of /Tgalactosidase (Hinek et al, 1993). Antibodies to these various laminin binding proteins have been shown to cross- react with each other, possibly due to common epitope structures (Risse et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Studies of the Structure of the Metastasis-Associated 67 kDa Laminin Binding Protein: Fatty Acid Acylation and Evidence Supporting Dimerization of the 32 kDa Gene Product To Form the Mature Protein

Landowski¹,

Dratz²,

Starkey³

1995

Biochemistry

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The level of expression of the 67 kDa high-affinity laminin binding protein (LBP) correlates with the progression of many solid tumors. The cDNA clone for the 67 kDa LBP is sufficient to encode a polypeptide of only 32 kDa, and there is no readily identifiable mechanism for membrane association. We have overexpressed the transfected 67 kDa hamster LBP in quantities that have enabled us to analyze the membrane-bound form of the protein. Treatment of the purified LBP with methyl transesterification reagents, followed by GC-MS, identified the covalently bound fatty acids palmitate, stearate, and oleate. The fatty acid modification may provide a mechanism for membrane association. Molecular mass determination by MALDI-TOF MS demonstrated the true molecular mass of the protein to be 66.7 kDa, compatible with the SDS-PAGE observation of 67 kDa. Treatment of the LBP with neuraminidase, O-glycanase, or Endo-F glycosidase has no detectable effect on the apparent molecular mass of the protein, and the MALDI-TOF MS did not show evidence of mass heterogeneities typically observed with glycosylated proteins. Reduction with dithiothreitol or beta-mercaptoethanol had no effect on the apparent molecular mass on SDS-PAGE or on the relative quantities of molecular mass species on MALDI-TOF MS. The experimentally determined amino acid composition, however, was found to be consistent with the 67 kDa form being a homodimer of the 32 kDa precursor. Preliminary experiments also suggest that the high-affinity laminin binding characteristic of the protein may be modulated by an, as yet, unidentified membrane accessory molecule.

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Section: Discussionmentioning

confidence: 99%

Studies of the Structure of the Metastasis-Associated 67 kDa Laminin Binding Protein: Fatty Acid Acylation and Evidence Supporting Dimerization of the 32 kDa Gene Product To Form the Mature Protein

Landowski¹,

Dratz²,

Starkey³

1995

Biochemistry

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“…The interaction of these molecules with their respective receptors in the cell membrane is known to induce alterations of cell morphology, possibly through a reorganization of the intracellular cytoskeleton [7,33,34]. The interaction of the ectoenzyme 5'-nucleotidase with fibronectin and laminin in vitro [11][12][13] and the possible existence of different isoforms of the ectoenzyme [5,9], linked to the cell membrane through a PI anchor [5,101 or through hydrophobic domains [1][2][3][4]8], suggest a role for the ectoenzyme as a cell receptor for the extracellular matrix [12,35] acting as a modulator of the adhesive properties and locomotion of cells [5].…”

Section: Discussionmentioning

confidence: 99%

“…In contrast, the inactivation of the ectoenzyme by fibronectin is not dependent on the 140 kDa fragment which is its cell-binding fragment [17]; only the 40 kDa fragment shows AMPase activity inhibition. This fragment binds gelatin and collagen and is involved in the fibrous polymerization of fibronectin [17,35].…”

Section: Discussionmentioning

confidence: 99%

Modulation of 5′-nucleotidase activity in plasma membranes and intact cells by the extracellular matrix proteins laminin and fibronectin

Olmo

Turnay

Risse

et al. 1992

Biochemical Journal

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Modulation of 5'-nucleotidase activity by the extracellular matrix proteins fibronectin, laminin and their fragments has been studied in plasma membrane preparations as well as in intact BCS-TC2 and Rugli cells. The ectoenzyme on plasma membranes is activated by laminin; fibronectin inhibits the AMPase activity on BCS-TC2 plasma membranes but no inhibitory effect is found in plasma membrane preparations from Rugli cells. These effects are dependent on the preincubation time and protein concentration. When the effect of the extracellular matrix proteins is studied on intact cells, both BCS-TC2 and Rugli cells show similar behaviour. A decrease in the enzyme activity is observed in the presence of fibronectin. The AMPase inhibitory activity is located on its 40 kDa fragment. No inhibitory activity is found in other fibronectin fragments, including the 140 kDa fragment which contains the RGDS cell-adhesion sequence. Laminin and its E1-4 and E8 fragments are able to activate the ecto-5'-nucleotidase activity of both BCS-TC2 and Rugli cells. The effect of the E1-4 fragment on intact cells is greater than that observed for the E8 fragment and uncleaved laminin. Our results suggest a bifunctional role for 5'-nucleotidase as ectoenzyme and cell receptor for extracellular matrix proteins.

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Isolation and characterization of 5′-nucleotidase of a human pancreatic tumor cell line

Flocke

Mannherz

1991

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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Structural comparison of the 68 kDa laminin-binding protein and 5′-nucleotidase from chicken muscular sources: Evidence against a gross structural similarity of both proteins

Cited by 7 publications

References 16 publications

Studies of the Structure of the Metastasis-Associated 67 kDa Laminin Binding Protein: Fatty Acid Acylation and Evidence Supporting Dimerization of the 32 kDa Gene Product To Form the Mature Protein

Studies of the Structure of the Metastasis-Associated 67 kDa Laminin Binding Protein: Fatty Acid Acylation and Evidence Supporting Dimerization of the 32 kDa Gene Product To Form the Mature Protein

Modulation of 5′-nucleotidase activity in plasma membranes and intact cells by the extracellular matrix proteins laminin and fibronectin

Isolation and characterization of 5′-nucleotidase of a human pancreatic tumor cell line

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