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F Prelli

Publications and source records attributed to F Prelli.

49 records · Page 3Linked to original sources
PubMed1981

A variant of prealbumin from amyloid fibrils in familial polyneuropathy of Jewish origin.

Amyloid fibrils were isolated from spleen and thyroid obtained at autopsy from one patient (S.K.O.) of Jewish origin with familial amyloidotic polyneuropathy. Gel filtration on Sephadex G100 after solubilization in 5 M guanidine HCl yielded three major components with 14,000, 9,000, and 5,000 mol wt, respectively. The two larger components shared antigenic determinants with human prealbumin. Amino acid analysis and amino terminal sequence studies revealed the 14,000-mol wt protein to be an intact prealbumin subunit. The 9,000-mol wt fragment obtained in highest yield encompassed the region from position 49-127 and the 5,000 mol wt fraction encompassed the amino terminal of prealbumin (position 1-48). An amino acid substitution (Gly/Thr) was detected at position 49, where enzymatic cleavage occurred. Thus, several prealbumin-derived fragments, predominantly the carboxyl end, constitute the amyloid fibrils in a heredofamilial amyloidosis syndrome of dominant inheritance.

Adult↗
PubMed1980

Primary structure of human gamma 3 immunoglobulin deletion mutant: gamma 3 heavy-chain disease protein Wis.

The complete sequence of a gamma 3 heavy-chain disease (HCD) protein Wis is presented. The molecule is a dimer of a 289-residue chain linked by 12 disulfide bonds. Protein Wis has an unusual amino terminus, followed by a deletion of most of the VH domain. After a small stretch homologous to the VC joining region, there is a second deletion which ends at the beginning of the quadruplicated hinge. Two carbohydrate groups are linked to Asn-6 and -140. the molecule has an extra interchain disulfide bridge at position 7 in addition to the 11 normally present in the quadruplicated hinge. The previously noted homology to the gamma 1 heavy chain is striking; from positions 224 to 234, protein Wis resembles gamma 1 Nei [Ponstingl, H., & Hilschmann, N. (1976) Hoppe-Seyler's Z. Physiol. Chem. 357, 1571--1604] except for a serine which replaces Asn at position 227. The results, taken together with studies of other immunoglobulin heavy-chain deletion mutants, support the suggestion that the different domains and interdomain regions of human H chains are coded for by different gene segments and that the deleted proteins reflect alterations in the recombination of different genes and/or the splicing of heterogeneous nuclear messenger ribonucleic acid (hn mRNA).

Amino Acid Sequence↗
PubMed1979

Human heavy chain disease protein WIS: implications for the organization of immunoglobulin genes.

Protein WIS is a human gamma3 heavy (H) chain disease immunoglobulin variant whose amino acid sequence is most readily interpreted by postulating that three residues of the amino terminus are followed by a deletion of most of the variable (VH) domain, which ends at the variable-constant (VC) joining region. Then there is a stretch of eight residues, three of which are unusual, while the other five have striking homology to the VC junction sequence. This is followed by a second deletion, which ends at the beginning of the quadruplicated hinge region. These findings are consistent with mutations resulting in deletions of most of the gene coding for the V region and CH1 domain followed by splicing at the VC joining region and at the hinge. These structural features fit well the notion of genetic discontinuity between V and C genes and also suggest similar mechanisms of excision and splicing in the interdomain regions of the C gene of the heavy chain.

Amino Acid Sequence↗
PubMed1976

Mu heavy-chain disease--a defect in immunoglobulin assembly. Structural studies of the kappa chain.

Mu-chain protein GLI is a pentameric molecule with an amino-terminal deletion comprising 130 residues. The half-cysteine residue (position 140) which forms the H-L disulfide bridge in normal IgM is present. Instead of being joined to the L chain, it presumably exists as an additional inter-H-H disulfide bridge. The kappa Bence Jones protein is of normal size and present in two forms: as monomers and dimers. The carboxy-terminal half-cysteine of the monomer is bound to cysteine. Possible reasons for failure of assembly between mu and L chains are briefly discussed.

Amino Acid Sequence↗
PubMed1976

The defect in mu heavy chain disease protein GLI.

Amino acid sequence studies of muHCD protein GLI reveal the absence of the amino terminal 130 residues. The molecule starts at Ala 131 and contains Cys 140, normally involved in the H-L disulfide bridges. Except for the deletion and presumably an extra H-H disulfide bridge involving Cys 140, the remainder of the mu-chain appears normal.

Amino Acid Sequence↗
PubMed1971

Interchain and intrachain disulfide bridges of a human immunoglobulin M: detection of a unique fragment.

Studies of the amino acid sequences around half-cystine residues in an immunoglobulin M have revealed an unexpectedly high number. At least 14 different sequences were found in the mu chain (V(HIII) subclass). Four of these were involved in interchain disulfide bridges and at least 10 in intrachain bridges. Five came from the kappa chain (kappa(III) subclass, Inv b). Several others, although having a high degree of homology, were not identical with those of either the mu or kappa chains. These results support the concept of an additional fragment in gammaM molecules, although its function and localization remain to be determined.

Amino Acid Sequence↗
PubMedDate not supplied

Amyloid arthropathy: characterization of the amyloid protein.

An 82 year-old man was referred for joint pain and numbness of his hands. Physical examination revealed limitation of movement of the PIP's, MCP's, wrists, shoulders and knees. There was marked synovial thickening of the wrists and atrophy of the thenar muscles of both hands due to arpal tunnel syndrome. The patient was operated on both hands, the median nerves were released and a synovectomy of the wrist was performed. Two months later, a synovectomy of the right shoulder was performed. Histological examination of tissues from the wrists and shoulder demonstrated large deposits of amyloid in the synovia. Amyloid fibrils were extracted, solubilized in 6M and were fractionated on a Sepharose 6B. All three proteins that were purified from the amyloid fibrils proved to be derived from VkI light chain by their amino terminal sequences. This is the first amyloid protein to be characterized from amyloid arthropathy.

Aged↗