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Results for “posttranslational modification”

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At least 289 records · Page 16Linked to original sources
PubMed1979

Studies of esterase 6 in Drosophila melanogaster. I. The genetics of a posttranslational modification.

A locus has been found, an allele of which causes a modification of some allozymes of the enzyme esterase 6 in Drosophila melanogaster. There are two alleles of this locus, one of which is dominant to the other and results in increased electrophoretic mobility of affected allozymes. The locus responsible has been mapped to 3-56.7 on the standard genetic map (Est-6 is at 3-36.8). Of 13 other enzyme systems analyzed, only leucine aminopeptidase is affected by the modifier locus. Neuraminidase incubations of homogenates altered the electrophoretic mobility of esterase 6 allozymes, but the mobility differences found are not large enough to conclude that esterase 6 is sialylated.

Alleles↗
PubMed1995

Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias.

The composition of collagen was analyzed and the degree of lysyl hydroxylation of individual collagen chains was determined in four osteosarcomas and two osteofibrous dysplasias. In addition, the tumor proliferation (number of mitoses, proliferating-nuclear-antigen-positive cells, MIB) as well as the response to chemotherapy (morphological regression grade) were checked. All tumors contained a high proportion of collagen III and, in all but one osteosarcoma, pepsin-extracted collagens I and III were overmodified. Furthermore, the proportion of diglycosides in collagen I was about four times higher than in controls. The collagen composition and modification resembled those of bones at early stages of human development. One osteosarcoma and both osteofibrous dysplasias were in the normal range of lysyl hydroxylation. There was no correlation between the collagen properties and the histopathological marker of tumor proliferation.

Adolescent↗
PubMedDate not supplied

Oxidative posttranslational modifications in Alzheimer disease. A possible pathogenic role in the formation of senile plaques and neurofibrillary tangles.

The distinctive pathological lesions of Alzheimer disease (AD), senile plaques, and neurofibrillary tangles comprise aggregates of insoluble fibrillar protein. We and other investigators recently demonstrated that several mechanisms related to oxidative stress and free-radical reactions could play a crucial role in the pathogenesis of AD and, specifically, in the formation of senile plaques and neurofibrillary tangles (NFT).

Alzheimer Disease↗
PubMed1988

Posttranslational modification of interleukin-2 is a late event during activation of human T lymphocytes by ionophore A23187 and phorbol ester.

Human peripheral blood lymphocytes secrete high titers of interleukin-2 (IL-2) after stimulation by Ca2+-ionophore A23187/phorbol 12-myristate-13-acetate. During the first 30 hours of incubation cells secrete only the nonglycosylated IL-2 M form of the lymphokine, the glycosylated forms IL-2 N1,2 being detected only after prolonged culture times (30-48 h). After recultivation of cells for a second 48 h period (without additional mitogen), the glycosylated and nonglycosylated IL-2 forms are secreted at a constant ratio of 7:3 throughout. The detection of glycosylated IL-2 is parallelled by an increase in cellular glycosyltransferase activities involved in formation of sialylated oligosaccharides O-linked to proteins.

Calcimycin↗
PubMed1992

A novel transglutaminase-catalyzed posttranslational modification of HIV-1 aspartyl protease.

We demonstrate that HIV-1 aspartyl protease (AP), the enzyme essential for the maturation of the AIDS virus, covalently incorporates spermidine catalyzed by guinea pig liver transglutaminase (TGase) and human coagulation factor XIIIa. Preliminary evidence indicates that there are at least three reactive glutamyl and lysyl residues in AP which act as acyl donor and acceptor respectively in a TGase reaction. SDS-PAGE and chromatographic analyses indicate that the two TGases tested catalyze the incorporation of radioactive spermidine into pure HIV-1 AP. The chemical identification and quantitation of (gamma-glutamyl) spermidine isopeptide provide conclusive evidence that the formation of this derivative is catalyzed by TGase. These results imply that TGase-catalyzed post-translational modification of HIV-1 AP may take place in a manner similar to the ones demonstrated in porcine pancreatic phospholipase A2.

Animals↗
PubMed1986

Acylated fibronectin: a new type of posttranslational modification of cellular fibronectin.

Human fibroblasts were labelled with either [35S]methionine or [3H]palmitate and analyzed for the presence of 35S- or 3H-labelled fibronectin by immunoprecipitation and SDS-polyacrylamide gel electrophoresis. The majority of 35S-labelled fibronectin was found in the extracellular matrix of cells which could be removed quantitatively by mild trypsin treatment. In contrast, 3H-labelled fibronectin was found in a trypsin-resistant form. The 3H label of fibronectin could be identified predominantly as [3H]palmitate by HLPC analysis. The fatty acids remained stably associated with fibronectin during extraction and electrophoresis, indicating a covalent linkage. These results demonstrate that a subset of fibronectin different from extracellular matrix fibronectin is modified by acylation.

Acylation↗
PubMed1993

A human synaptic vesicle monoamine transporter cDNA predicts posttranslational modifications, reveals chromosome 10 gene localization and identifies TaqI RFLPs.

A human vesicular monoamine transporter cDNA has been identified by screening a human brainstem library using sequences from the rat brain synaptic vesicle monoamine transporter (SVMT) [(1992) Cell 70, 539-551; (1992) Proc. Natl. Acad. Sci. USA 89, 10993-10997]. The hSVMT shares 92% amino acid identity with the rat sequence, but displays one less consensus site for asparagine N-linked glycosylation and one more consensus site for phosphorylation by protein kinase C. The human SVMT gene maps to chromosome 10q25 using Southern blotting analysis of human/rodent hybrid cell lines and fluorescent in situ hybridization approaches. The cDNA, and a subclone, recognize TaqI polymorphisms that may prove useful to assess this gene's involvement in neuropsychiatric disorders involving monoaminergic brain systems.

Amino Acid Sequence↗
PubMed1995

Boar spermadhesin PSP-II: location of posttranslational modifications, heterodimer formation with PSP-I glycoforms and effect of dimerization on the ligand-binding capabilities of the subunits.

Spermadhesin PSP-II was isolated from the non-heparin-binding fraction of boar seminal plasma; its disulphide bridge pattern, and the location of a single N-glycosylation site were established. PSP-II forms a heterodimer with specific N-glycoforms of PSP-I. Although both subunits possess heparin-binding capability, the PSP-I/PSP-II complex does not. The heterodimer contains binding sites for zona pellucida glycoproteins and soybean trypsin inhibitor located in the PSP-II subunit. However, the PSP-I/PSP-II heterodimer binds only loosely to the sperm surface and is easily removed during in vitro capacitation, suggesting that the zona pellucida binding activity may not be relevant for gamete interaction. Our results show that dimerization of spermadhesins PSP-I and PSP-II markedly affects their binding capabilities.

Amino Acid Sequence↗
PubMed1988

Neurofilament triplet proteins of NB2a/d1 neuroblastoma: posttranslational modification and incorporation into the cytoskeleton during differentiation.

Induction of axonal neuritogenesis in NB2a/d1 cells was associated with an increased content of neurofilament proteins (NFPs) by immunoblot analysis. The major NFP subunits in differentiated [NB2a(+)] cells included microheterogenous forms with apparent molecular weights of 200-190 kDa (NFP-H), 143-142 kDa (NFP-M) and 70 kDa (NFP-L) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Only NFP-L was detected in cytoskeletal preparations of undifferentiated [NB2a(-)] cells. All three NFPs of NB2a(+) cells incorporated 32P-orthophosphate in intact cells. A 160/155 kDa NFP-H immunoreactive polypeptide in NB2a(-) and NB2a(+) cells represented a relatively unmodified form of the 200 kDa NFP-H, since dephosphorylation of the 200 kDa NFP-H in vitro with alkaline phosphatase generated the 160/155 kDa forms. Triton-extracted NB2a(+) cells displayed NFP-H immunoreactivity in neurites and occasionally in perikaryal regions at the base of neurites. NFP-M was present throughout the neurites and somata of NB2a(+) cells, and was regularly detected in portions of perikarya in NB2a(-) cells. NFP-L immunoreactivity was distributed throughout the Triton-insoluble cytoskeleton of NB2a(-) and NB2a(+) cells. Immunocytochemical analyses revealed that extensively phosphorylated forms of NFP-H were largely restricted to the neurites of NB2a(+) cells, and less modified forms predominated throughout both perikarya and neurites of NB2a(-) and NB2a(+) cells.

Animals↗
PubMed1995

Posttranslational modification of protein kinase A. The link between short-term and long-term memory.

Both for Aplysia and Drosophila a key role in the molecular mechanism of learning and memory processes has been assigned to the cAMP cascade. In any learning process a short-time stimulus has to be translated into long-lasting changes. The molecular correlate must be a cascade of biochemical reactions with different kinetics, functionally interlinked and operating in overlapping time ranges. Biochemical studies in Drosophila have led to the suggestion that one of these steps is a proteolytic modification of the regulatory subunits of protein kinase A. A quantitative analysis of the relaxation kinetics of a system of protein kinase A, phosphatases and a calcium-dependent protease can give an image of essential characteristics of learning behaviour in Drosophila.

Animals↗
PubMed2004

Ostrich (Struthio camelus) eggshell matrix contains two different C-type lectin-like proteins. Isolation, amino acid sequence, and posttranslational modifications.

In contrast to chicken and goose, the ostrich calcified eggshell layer matrix contained two different C-type lectin-like proteins as major components. These proteins, named struthiocalcin-1 (SCA-1) and struthiocalcin-2 (SCA-2), were isolated and their amino acid sequence was determined. SCA-1 clearly was the ortholog of goose eggshell ansocalcin. Its amino acid sequence had the same length as that of ansocalcin (132 aa) and showed 65% sequence identity with the goose eggshell protein compared to 41% with chicken eggshell ovocleidin-17. Furthermore, as ansocalcin and unlike ovocleidin-17, it contained an additional, seventh, cysteine that was, however, located close to the C-terminus of SCA-1 and not in the N-terminal third of the sequence as in ansocalcin. SCA-2 showed features of both ansocalcin and chicken eggshell ovocleidin-17 (OC-17). Its sequence was 46% identical to that of ansocalcin and 36% identical to OC-17. It contained the same stretches of negatively charged amino acids conserved in ansocalcin and SCA-1, which are absent in OC-17. On the other hand, its length of 142 amino acids was identical to that of OC-17 and it contained only the usual set of six cysteines conserved in most C-type lectin-like proteins. The presence of three phosphorylated serines located at exactly the same region of the sequence as the two phosphoserines of OC-17 further stressed the similarity between SCA-2 and OC-17.

Amino Acid Sequence↗