Transcalciferin in serum and cytosol

Bouillon, Roger; Baelen, Hugo Van; Demoor, P

doi:10.1007/bf02064097

Cited by 4 publications

(10 citation statements)

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“…Plasma from patients heterozygous for the mutation showed significantly lower activities, about 50% of control values. We were unable to show whether the actin monomer binding activity of the mutant gelsolin is also reduced, because plasma contains high concentrations of vitamin D binding protein, which also binds monomeric actin [18]. This can be seen in Fig.…”

Section: Discussionmentioning

confidence: 86%

“…In addition to gelsolin, plasma contains high concentrations of vitamin-D binding protein [18], which sequesters monomeric actin; thus F-actin would be expected to be depolymerized, albeit more slowly [26]. Loss of activity by cytoplasmic gelsolin is likely to be much more serious if gelsolin plays an essential role in cell locomotion and motility [27].…”

Section: Discussionmentioning

confidence: 99%

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Variant plasma gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity

et al. 1993

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Familial amyloidosis, Finnish type is caused by a single base mutation in gelsolin, an actin filament severing and capping protein that is present in most tissues and in blood plasma. The mutation replaces aspartic acid with asparagine at residue 187 of the plasma sequence. This renders the gelsolin susceptible to proteolysis as a consequence of which amyloid protein is formed. Here it is shown that the mutant protein in plasma from a patient homozygous for this mutation lacks both actin severing and nucleating activities. Evidence is presented that the cleaved mutant gelsolin has dissociated under non‐denaturing conditions and that the resultant 65,000 and 55,000 M r C‐terminal fragments aggregate.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Variant plasma gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity

et al. 1993

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“…These data agree with the findings of Haddad and Walgate (14) that antiserum developed to hDBP did not cross-react with rat DBP, but showed limited cross-reactivity with primate and porcine DBP. Bouillon et al (1) found that anti-rat DBP antiserum did not cross-react with DBP from human, monkey, dog, and rabbit. Numerous antisera to DBP from a number of species, including humans, have been produced to date (1,14).…”

Section: Resultsmentioning

confidence: 99%

“…Vitamin D and its metabolites are transported in the circulation bound to a specific binding protein, vitamin D-binding protein (DBP) (1). Although a number of hypotheses have been advanced regarding its function (2,3), thus far the only action of DBP that has received experimental support is that of a serum carrier for vitamin D metabolites (4).…”

mentioning

confidence: 99%

Monoclonal antibodies to human vitamin D-binding protein.

Pierce¹,

Dame²,

Bouillon³

et al. 1985

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

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“…The human plasma vitamin D-binding protein (DBP)' is a 58,000-D interalpha globulin possessing one sterol binding site per molecule (1)(2)(3). 25-hydroxycholecalciferol is bound with the highest affinity (10-8 M), but normally occupies < 5% of available binding sites (4).…”

Section: Introductionmentioning

confidence: 99%

Vitamin D binding protein sequesters monomeric actin in the circulation of the rat.

Harper¹,

McLeod²,

Kowalski³

et al. 1987

J. Clin. Invest.

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Plasma vitamin D binding protein (DBP) may scavenge actin released during cell lysis. We examined the plasma disappearance and tissue appearance of '"I-DBP, '2I-G-actin, and the DBP-G-actin complex after their intravenous administration to rats. The plasma disappearance of DBP and DBP-actin were indistinguishable, with rapid initial (tl/2 = 2.6 h) and slower second (t/2 = 7 h) slopes. After 125I-G-actin (nanomole) injection, plasma disappearance paralleled that of DBP and DBP-actin. All injected actin was associated with DBP, without evidence of free actin, actin-gelsolin complexes or actin oligomers. Tissue appearances of 1251I-apolipoprotein (apo) or holo-DBP were similar, with highest accumulations in perfused liver, kidney, and skeletal muscle. Although more complex phenomena (plasma entry of F-actin and intracellular actin binding proteins) would occur in vivo after cell lysis, our results suggest a role for DBP in the sequestration and disposition of actin monomers in the circulation.

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Transcalciferin in serum and cytosol

Cited by 4 publications

References 4 publications

Variant plasma gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity

Variant plasma gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity

Monoclonal antibodies to human vitamin D-binding protein.

Vitamin D binding protein sequesters monomeric actin in the circulation of the rat.

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