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Volumn 1771, Issue 1, 2007, Pages 55-65

Purification, cloning and regulation of a novel acid-lipase-like protein of hamster expressed in lacrimal glands and tears during lactation

Author keywords

Acid lipase; Harderian gland; Lacrimal gland; Lactation; Lipocalin; Sex hormone; Syrian hamster; Tear film lipid; Thyroid hormone

Indexed keywords

ACID LIPASE; ANDROGEN; COMPLEMENTARY DNA; ESTROGEN; LIPID BINDING PROTEIN; POLYMER; TEAR PROTEIN; THYROID HORMONE; TRIACYLGLYCEROL LIPASE;

EID: 33846056541     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.10.002     Document Type: Article
Times cited : (6)

References (56)
  • 1
    • 0019426669 scopus 로고
    • Clinical biochemistry of tears
    • Van Haeringen N.J. Clinical biochemistry of tears. Surv. Ophthalmol. 26 (1981) 84-96
    • (1981) Surv. Ophthalmol. , vol.26 , pp. 84-96
    • Van Haeringen, N.J.1
  • 2
    • 0028217972 scopus 로고
    • Composition and biophysical properties of the tear film: knowledge and uncertainty
    • Tiffany J.M. Composition and biophysical properties of the tear film: knowledge and uncertainty. Adv. Exp. Med. Biol. 350 (1994) 231-238
    • (1994) Adv. Exp. Med. Biol. , vol.350 , pp. 231-238
    • Tiffany, J.M.1
  • 3
    • 3042530909 scopus 로고    scopus 로고
    • Changes in the tear film and ocular surface from dry eye syndrome
    • Johnson M.E., and Murphy P.J. Changes in the tear film and ocular surface from dry eye syndrome. Prog. Retin. Eye Res. 23 (2004) 449-474
    • (2004) Prog. Retin. Eye Res. , vol.23 , pp. 449-474
    • Johnson, M.E.1    Murphy, P.J.2
  • 6
    • 0029998753 scopus 로고    scopus 로고
    • Sexual diversity of the lipid metabolism in the Harderian gland of the golden hamster
    • Seyama Y., Otsuka H., Ohashi K., Vivien-Roels B., and Pevet P. Sexual diversity of the lipid metabolism in the Harderian gland of the golden hamster. Microsc. Res. Tech. 34 (1996) 71-76
    • (1996) Microsc. Res. Tech. , vol.34 , pp. 71-76
    • Seyama, Y.1    Otsuka, H.2    Ohashi, K.3    Vivien-Roels, B.4    Pevet, P.5
  • 7
    • 27844568472 scopus 로고    scopus 로고
    • Human tear viscosity: an interactive role for proteins and lipids
    • Gouveia S.M., and Tiffany J.M. Human tear viscosity: an interactive role for proteins and lipids. Biochim. Biophys. Acta 1753 (2005) 155-163
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 155-163
    • Gouveia, S.M.1    Tiffany, J.M.2
  • 8
    • 0034684199 scopus 로고    scopus 로고
    • Human tear lipocalin
    • Redl B. Human tear lipocalin. Biochim. Biophys. Acta 1482 (2000) 241-248
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 241-248
    • Redl, B.1
  • 9
    • 21744434036 scopus 로고    scopus 로고
    • cDNA cloning and regulation of two sex-hormone-repressed hamster tear lipocalins having homology with odorant/pheromone-binding proteins
    • Srikantan S., Parekh V., and De P.K. cDNA cloning and regulation of two sex-hormone-repressed hamster tear lipocalins having homology with odorant/pheromone-binding proteins. Biochim. Biophys. Acta 1729 (2005) 154-165
    • (2005) Biochim. Biophys. Acta , vol.1729 , pp. 154-165
    • Srikantan, S.1    Parekh, V.2    De, P.K.3
  • 10
    • 0032954406 scopus 로고    scopus 로고
    • Pancreatic lipase-related protein 1 mRNA in female mouse lacrimal gland
    • Remington S.G., Lima P.H., and Nelson J.D. Pancreatic lipase-related protein 1 mRNA in female mouse lacrimal gland. Invest Ophthalmol. Visual Sci. 40 (1999) 1081-1090
    • (1999) Invest Ophthalmol. Visual Sci. , vol.40 , pp. 1081-1090
    • Remington, S.G.1    Lima, P.H.2    Nelson, J.D.3
  • 11
    • 0036906051 scopus 로고    scopus 로고
    • mRNA encoding a new lipolytic enzyme expressed in rabbit lacrimal glands
    • Remington S.G., and Nelson J.D. mRNA encoding a new lipolytic enzyme expressed in rabbit lacrimal glands. Invest Ophthalmol. Visual Sci. 43 (2002) 3617-3624
    • (2002) Invest Ophthalmol. Visual Sci. , vol.43 , pp. 3617-3624
    • Remington, S.G.1    Nelson, J.D.2
  • 12
    • 0036820456 scopus 로고    scopus 로고
    • Lipid, lipase and lipocalin differences between tolerant and intolerant contact lens wearers
    • Glasson M., Stapleton F., and Willcox M. Lipid, lipase and lipocalin differences between tolerant and intolerant contact lens wearers. Curr. Eye Res. 25 (2002) 227-235
    • (2002) Curr. Eye Res. , vol.25 , pp. 227-235
    • Glasson, M.1    Stapleton, F.2    Willcox, M.3
  • 15
    • 0030770787 scopus 로고    scopus 로고
    • Influence of various signal peptides on secretion of mammalian acidic lipases in baculovirus-insect cell system
    • Dupuis L., Canaan S., Riviere M., and Wicker-Planquart C. Influence of various signal peptides on secretion of mammalian acidic lipases in baculovirus-insect cell system. Methods Enzymol. 284 (1997) 261-272
    • (1997) Methods Enzymol. , vol.284 , pp. 261-272
    • Dupuis, L.1    Canaan, S.2    Riviere, M.3    Wicker-Planquart, C.4
  • 17
    • 0023829203 scopus 로고
    • Lingual and gastric lipases: species differences in the origin of prepancreatic digestive lipases and in the localization of gastric lipase
    • DeNigris S.J., Hamosh M., Kasbekar D.K., Lee T.C., and Hamosh P. Lingual and gastric lipases: species differences in the origin of prepancreatic digestive lipases and in the localization of gastric lipase. Biochim. Biophys. Acta 959 (1988) 38-45
    • (1988) Biochim. Biophys. Acta , vol.959 , pp. 38-45
    • DeNigris, S.J.1    Hamosh, M.2    Kasbekar, D.K.3    Lee, T.C.4    Hamosh, P.5
  • 18
    • 0025791980 scopus 로고
    • Cloning and expression of cDNA encoding human lysosomal acid lipase/cholesteryl ester hydrolase. Similarities to gastric and lingual lipases
    • Anderson R.A., and Sando G.N. Cloning and expression of cDNA encoding human lysosomal acid lipase/cholesteryl ester hydrolase. Similarities to gastric and lingual lipases. J. Biol. Chem. 266 (1991) 22479-22484
    • (1991) J. Biol. Chem. , vol.266 , pp. 22479-22484
    • Anderson, R.A.1    Sando, G.N.2
  • 19
    • 0034721518 scopus 로고    scopus 로고
    • Difference in substrate specificity between human and mouse lysosomal acid lipase: low affinity for cholesteryl ester in mouse lysosomal acid lipase
    • Groener J.E., Bax W., Stuani C., and Pagani F. Difference in substrate specificity between human and mouse lysosomal acid lipase: low affinity for cholesteryl ester in mouse lysosomal acid lipase. Biochim. Biophys. Acta 1487 (2000) 155-162
    • (2000) Biochim. Biophys. Acta , vol.1487 , pp. 155-162
    • Groener, J.E.1    Bax, W.2    Stuani, C.3    Pagani, F.4
  • 22
    • 0030983202 scopus 로고    scopus 로고
    • Human lysosomal acid lipase/cholesteryl ester hydrolase and human gastric lipase: identification of the catalytically active serine, aspartic acid, and histidine residues
    • Lohse P., Chahrokh-Zadeh S., Lohse P., and Seidel D. Human lysosomal acid lipase/cholesteryl ester hydrolase and human gastric lipase: identification of the catalytically active serine, aspartic acid, and histidine residues. J. Lipid Res. 38 (1997) 892-903
    • (1997) J. Lipid Res. , vol.38 , pp. 892-903
    • Lohse, P.1    Chahrokh-Zadeh, S.2    Lohse, P.3    Seidel, D.4
  • 25
    • 0033485708 scopus 로고    scopus 로고
    • Abundant secretory lipocalins displaying male and lactation-specific expression in adult hamster submandibular gland. cDNA cloning and sex hormone-regulated repression
    • Thavathiru E., Jana N.R., and De P.K. Abundant secretory lipocalins displaying male and lactation-specific expression in adult hamster submandibular gland. cDNA cloning and sex hormone-regulated repression. Eur. J. Biochem. 266 (1999) 467-476
    • (1999) Eur. J. Biochem. , vol.266 , pp. 467-476
    • Thavathiru, E.1    Jana, N.R.2    De, P.K.3
  • 27
    • 0029942665 scopus 로고    scopus 로고
    • Inhibition studies on calf pregastric esterase: the enzyme has no functional thiol group
    • Timmermans M.Y., Reekmans G., Teuchy H.J., and Kupers L.P. Inhibition studies on calf pregastric esterase: the enzyme has no functional thiol group. Biochem. J. 314 (1996) 931-936
    • (1996) Biochem. J. , vol.314 , pp. 931-936
    • Timmermans, M.Y.1    Reekmans, G.2    Teuchy, H.J.3    Kupers, L.P.4
  • 28
    • 0038352222 scopus 로고    scopus 로고
    • In vitro lipolysis by human pancreatic lipase is specifically abolished by its inactive forms
    • Miled N., Berti-Dupuis L., Riviere M., Carriere F., and Verger R. In vitro lipolysis by human pancreatic lipase is specifically abolished by its inactive forms. Biochim. Biophys. Acta 1645 (2003) 241-246
    • (2003) Biochim. Biophys. Acta , vol.1645 , pp. 241-246
    • Miled, N.1    Berti-Dupuis, L.2    Riviere, M.3    Carriere, F.4    Verger, R.5
  • 29
    • 0035827661 scopus 로고    scopus 로고
    • Revisiting the specificity of Mamestra brassicae and Antheraea polyphemus pheromone-binding proteins with a fluorescence binding assay
    • Campanacci V., Krieger J., Bette S., Sturgis J.N., Lartigue A., Cambillau C., Breer H., and Tegoni M. Revisiting the specificity of Mamestra brassicae and Antheraea polyphemus pheromone-binding proteins with a fluorescence binding assay. J. Biol. Chem. 27 (2001) 20078-20084
    • (2001) J. Biol. Chem. , vol.27 , pp. 20078-20084
    • Campanacci, V.1    Krieger, J.2    Bette, S.3    Sturgis, J.N.4    Lartigue, A.5    Cambillau, C.6    Breer, H.7    Tegoni, M.8
  • 30
    • 0028923036 scopus 로고
    • Androgens and estrogens markedly inhibit expression of a 20-kDa major protein in hamster exorbital lacrimal gland
    • Ranganathan V., and De P.K. Androgens and estrogens markedly inhibit expression of a 20-kDa major protein in hamster exorbital lacrimal gland. Biochem. Biophys. Res. Commun. 208 (1995) 412-417
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 412-417
    • Ranganathan, V.1    De, P.K.2
  • 31
    • 0032704543 scopus 로고    scopus 로고
    • Hormonal effects on hamster lacrimal gland female-specific major 20-kDa secretory protein and its immunological similarity with submandibular gland major male-specific proteins
    • Ranganathan V., Jana N.R., and De P.K. Hormonal effects on hamster lacrimal gland female-specific major 20-kDa secretory protein and its immunological similarity with submandibular gland major male-specific proteins. J. Steroid Biochem. Mol. Biol. 70 (1999) 151-158
    • (1999) J. Steroid Biochem. Mol. Biol. , vol.70 , pp. 151-158
    • Ranganathan, V.1    Jana, N.R.2    De, P.K.3
  • 32
    • 0033564008 scopus 로고    scopus 로고
    • Site-directed removal of N-glycosylation sites in human gastric lipase
    • Wicker-Planquart C., Canaan S., Riviere M., and Dupuis L. Site-directed removal of N-glycosylation sites in human gastric lipase. Eur. J. Biochem. 262 (1999) 644-651
    • (1999) Eur. J. Biochem. , vol.262 , pp. 644-651
    • Wicker-Planquart, C.1    Canaan, S.2    Riviere, M.3    Dupuis, L.4
  • 33
    • 18244385491 scopus 로고    scopus 로고
    • Systematic mutagenesis of potential glycosylation sites of lysosomal acid lipase
    • Zschenker O., Bahr C., Hess U.F., and Ameis D. Systematic mutagenesis of potential glycosylation sites of lysosomal acid lipase. J. Biochem. (Tokyo) 137 (2005) 387-394
    • (2005) J. Biochem. (Tokyo) , vol.137 , pp. 387-394
    • Zschenker, O.1    Bahr, C.2    Hess, U.F.3    Ameis, D.4
  • 35
    • 0027990685 scopus 로고
    • The cDNA sequence encoding bovine pregastric esterase
    • Timmermans M.Y., Teuchy H., and Kupers L.P. The cDNA sequence encoding bovine pregastric esterase. Gene 147 (1994) 259-262
    • (1994) Gene , vol.147 , pp. 259-262
    • Timmermans, M.Y.1    Teuchy, H.2    Kupers, L.P.3
  • 38
    • 0028862871 scopus 로고
    • Cloning of rat lysosomal acid lipase cDNA and identification of the mutation in the rat model of Wolman's disease
    • Nakagawa H., Matsubara S., Kuriyama M., Yoshidome H., Fujiyama J., Yoshida H., and Osame M. Cloning of rat lysosomal acid lipase cDNA and identification of the mutation in the rat model of Wolman's disease. J. Lipid Res. 36 (1995) 2212-2218
    • (1995) J. Lipid Res. , vol.36 , pp. 2212-2218
    • Nakagawa, H.1    Matsubara, S.2    Kuriyama, M.3    Yoshidome, H.4    Fujiyama, J.5    Yoshida, H.6    Osame, M.7
  • 39
    • 0033546322 scopus 로고    scopus 로고
    • Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest
    • Roussel A., Canaan S., Egloff M.P., Riviere M., Dupuis L., Verger R., and Cambillau C. Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J. Biol. Chem. 274 (1999) 16995-17002
    • (1999) J. Biol. Chem. , vol.274 , pp. 16995-17002
    • Roussel, A.1    Canaan, S.2    Egloff, M.P.3    Riviere, M.4    Dupuis, L.5    Verger, R.6    Cambillau, C.7
  • 41
    • 0032575265 scopus 로고    scopus 로고
    • An enzymatically active truncated form (- 55 N-terminal residues) of rabbit gastric lipase. Correlation between the enzymatic activity and disulfide bond oxydo-reduction state
    • de Caro J., Verger R., and de Caro A. An enzymatically active truncated form (- 55 N-terminal residues) of rabbit gastric lipase. Correlation between the enzymatic activity and disulfide bond oxydo-reduction state. Biochim. Biophys. Acta 1386 (1998) 39-49
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 39-49
    • de Caro, J.1    Verger, R.2    de Caro, A.3
  • 42
    • 0030924426 scopus 로고    scopus 로고
    • Cysteine residues in human lysosomal acid lipase are involved in selective cholesteryl esterase activity
    • Pagani F., Pariyarath R., Stuani C., Garcia R., and Baralle F.E. Cysteine residues in human lysosomal acid lipase are involved in selective cholesteryl esterase activity. Biochem. J. 326 (1997) 265-269
    • (1997) Biochem. J. , vol.326 , pp. 265-269
    • Pagani, F.1    Pariyarath, R.2    Stuani, C.3    Garcia, R.4    Baralle, F.E.5
  • 44
    • 0034917245 scopus 로고    scopus 로고
    • Reductions in hamster serum thyroxine levels by melatonin are not altered by changes in serum testosterone
    • Champney T.H. Reductions in hamster serum thyroxine levels by melatonin are not altered by changes in serum testosterone. Gen. Comp Endocrinol. 123 (2001) 121-126
    • (2001) Gen. Comp Endocrinol. , vol.123 , pp. 121-126
    • Champney, T.H.1
  • 45
    • 0016242332 scopus 로고
    • Plasma levels of oestrogen and progesterone in pregnant and lactating hamsters
    • Baranczuk R., and Greenwald G.S. Plasma levels of oestrogen and progesterone in pregnant and lactating hamsters. J. Endocrinol. 63 (1974) 125-135
    • (1974) J. Endocrinol. , vol.63 , pp. 125-135
    • Baranczuk, R.1    Greenwald, G.S.2
  • 46
    • 0002089756 scopus 로고
    • The estrous cycle
    • Siegel H.I. (Ed), Plenum Press, New York
    • Lisk R.D. The estrous cycle. In: Siegel H.I. (Ed). The Hamster, Reproduction and Behaviour (1985), Plenum Press, New York 23-51
    • (1985) The Hamster, Reproduction and Behaviour , pp. 23-51
    • Lisk, R.D.1
  • 47
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda A., and Pascual A. Nuclear hormone receptors and gene expression. Physiol. Rev. 81 (2001) 1269-1304
    • (2001) Physiol. Rev. , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 49
    • 11144300156 scopus 로고    scopus 로고
    • Cyclorraphan yolk proteins and lepidopteran minor yolk proteins originate from two unrelated lipase families
    • Hens K., Lemey P., Macours N., Francis C., and Huybrechts R. Cyclorraphan yolk proteins and lepidopteran minor yolk proteins originate from two unrelated lipase families. Insect Mol. Biol. 13 (2004) 615-623
    • (2004) Insect Mol. Biol. , vol.13 , pp. 615-623
    • Hens, K.1    Lemey, P.2    Macours, N.3    Francis, C.4    Huybrechts, R.5
  • 51
    • 0026655197 scopus 로고
    • Why is there sequence similarity between insect yolk proteins and vertebrate lipases?
    • Bownes M. Why is there sequence similarity between insect yolk proteins and vertebrate lipases?. J. Lipid Res. 33 (1992) 777-790
    • (1992) J. Lipid Res. , vol.33 , pp. 777-790
    • Bownes, M.1
  • 53
    • 33646477172 scopus 로고    scopus 로고
    • Pancreatic lipase and pancreatic lipase-related protein 2, but not pancreatic lipase-related protein 1, hydrolyze retinyl palmitate in physiological conditions
    • Reboul E., Berton A., Moussa M., Kreuzer C., Crenon I., and Borel P. Pancreatic lipase and pancreatic lipase-related protein 2, but not pancreatic lipase-related protein 1, hydrolyze retinyl palmitate in physiological conditions. Biochim. Biophys. Acta 1761 (2006) 4-10
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 4-10
    • Reboul, E.1    Berton, A.2    Moussa, M.3    Kreuzer, C.4    Crenon, I.5    Borel, P.6
  • 55
    • 27144557079 scopus 로고    scopus 로고
    • Sex-specific peptides from exocrine glands stimulate mouse vomeronasal sensory neurons
    • Kimoto H., Haga S., Sato K., and Touhara K. Sex-specific peptides from exocrine glands stimulate mouse vomeronasal sensory neurons. Nature 437 (2005) 898-901
    • (2005) Nature , vol.437 , pp. 898-901
    • Kimoto, H.1    Haga, S.2    Sato, K.3    Touhara, K.4
  • 56
    • 0032944085 scopus 로고    scopus 로고
    • The mother rat's vomeronasal organ is involved in detection of dodecyl propionate, the pup's preputial gland pheromone
    • Brouette-Lahlou I., Godinot F., and Vernet-Maury E. The mother rat's vomeronasal organ is involved in detection of dodecyl propionate, the pup's preputial gland pheromone. Physiol. Behav. 66 (1999) 427-436
    • (1999) Physiol. Behav. , vol.66 , pp. 427-436
    • Brouette-Lahlou, I.1    Godinot, F.2    Vernet-Maury, E.3


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