Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase

Huang, Kuo‐Sen; Wallner, Barbara; Mattaliano, Robert J.; Tizard, Richard; Burne, C; Frey, Alexis Z.; Hession, Catherine; McGray, Paula; Sinclair, L K; Chow, E P; Browning, Jeffrey L.; Ramachandran, K L; Tang, John C.-T.; Smart, John E.; Pepinsky, R. Blake

doi:10.1016/0092-8674(86)90736-1

Cited by 416 publications

(210 citation statements)

References 31 publications

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“…Partial double stranded cDNA sequencing of the subcloned 1.0 and 0.4 kb EcoRI fragments indicated that the three clones isolated were derived from the same cDNA insert. A search of the GenBank DNA sequence database revealed a perfect match with human calpactin I (heavy chain) (accession # M14043) (Saris et al, 1986) and lipocortin II (accession # A23942) (Huang et al, 1986), proteins also known as annexin II and p36. Further confirmation of the identity of the 3.186 cDNA clone was obtained by restriction endonuclease mapping with AccI, NdeI, HincIl, HindIll, PstI and XbaI.…”

Section: Resultsmentioning

confidence: 99%

“…The NH2-terminal tails of the annexins are quite variable in sequence and length. In p36 (annexin II), this region contains both serine and tyrosine phosphorylation sites (Glenney & Tack, 1985;Gerke, 1989) and p36 has been shown to be a substrate for pp6Ov-src (Huang et al, 1986;Erikson et al, 1984;Saris et al, 1986) and protein kinase C (Gould et al, 1986;Barnes et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

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Elevated expression of Annexin II (Lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line

Cole

Pinkoski²,

Bhardwaj³

et al. 1992

Br J Cancer

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Elevated expression of Annexin II (Lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line

Cole

Pinkoski²,

Bhardwaj³

et al. 1992

Br J Cancer

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“…In addition to direct and indirect analyses of fragments by CNBr mapping ( fig.2), we tried to localize the epitope by cleaving lipocortin with elastase under limiting conditions [18] and then using the antibodies to immuneprecipitate functional fragments. None of the fragments were detected.…”

Section: Resultsmentioning

confidence: 99%

“…"Slabeled lipocortin-1 was produced in the same strain, using cells that were adapted to grow in low sulphate medium. A 50 ml culture was grown in the presence of 10 mCi ["S]sulphate and labeled lipocortin purified as previously described [17,18]. Human, rat, and bovine lipocortins l-6 were purified as described [1,2].…”

Section: Purificatioi Of L~~~o~t~~-like Proteinsmentioning

confidence: 99%

Monoclonal antibodies to lipocortin‐1 as probes for biological function

Pepinsky¹,

Sinclair²,

Dougas³

et al. 1990

FEBS Letters

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We have developed two monoclonal antibodies to human lipocortin-1 (103 and 105) as reagents for quantitating the protein in biological systems and neutralizing its activity. Lipo 105 is a high affinity antibody that is functional in ELISA and Western blot formats. The antibody recognizes a site between amino acids 30 and 55 in the lipocortin-I sequence and can be used on native or denatured protein. Lipo 103 is an antibody that neutralizes the phospholipase A, inhibitory activity of lipocortin-1 by blocking binding of the protein to phospholipid surfaces. The antibody is specific for native human lipocortin-1. Lipo 103 was recently shown to block lipocortin-l-dependent differentiation of a squamous carcinoma cell line, demonstrating its usefulness as a probe for function.

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“…Lipocortins are a family of calcium and phospholopid binding proteins described initially as glucocorticoid-induced and secreted proteins inhibiting phospholipase A2 in vitro and in vivo [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15], and thus preventing the release of inflammatory mediators, prostaglandin E2 and leukotrienes. Human respiratory diseases including acute and chronic bronchitis, asthma and cystic fibrosis are associated with excessive airway mucus production, mainly originating from submucosal gland secretory cells [6,7].…”

Section: Introductionmentioning

confidence: 99%

Production of lipocortin‐like proteins by cultured human tracheal submucosal gland cells

Jacquot

Dupuit

Elbtaouri³

et al. 1990

FEBS Letters

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Evidence is obtained for the presence of lipocortin-like proteins in human tracheal gland cells in culture. Using polyclonal antibodies to lipocortin I, indirect immunofluorescence studies demonstrate that lipocortin I is mainly confined to the tracheal gland cell surface. From cell membranes, four Ca2+-dependent proteins (35, 40, 45 and 67 kDa) were identified as lipocortin related proteins by using immunoblotting and fluorography following [35S]methionine metabolic labeling experiments. A strong immunoreactivity for the 35 kDa protein was observed. In addition, lipocortinlike proteins with apparent Mr33, 35, 37 and 67 kDa, respectively, were released in the apical culture medium by tracheal gland cells cultured on microporous membrane of a double chamber culture system.

show abstract

Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase

Cited by 416 publications

References 31 publications

Elevated expression of Annexin II (Lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line

Elevated expression of Annexin II (Lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line

Monoclonal antibodies to lipocortin‐1 as probes for biological function

Production of lipocortin‐like proteins by cultured human tracheal submucosal gland cells

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