Dog and Rat Pancreatic Phospholipases A2: Complete Amino Acid Sequences Deduced from Complementary DNAs

Ohara, Osamu; Tamaki, Mikio; Nakamura, Etsuo; Tsuruta, Yuji; Fujii, Yoko; Shin, Masaru; Teraoka, Hiroshi; Okamoto, Mitsuhiro

doi:10.1093/oxfordjournals.jbchem.a135532

Cited by 94 publications

(27 citation statements)

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“…The Westernblot analysis confirmed that the 14-kDa protein is hPLA2-I. The N-terminal 20 amino acids sequence of the isolated hPLA2-I was identical with that of the mature hPLA2-I reported previously [20].…”

Section: Purification Of Hpla2-i From Human Pancreatic Juicesupporting

confidence: 79%

Human pancreatic phospholipase A₂ stimulates the growth of human pancreatic cancer cell line

Hanada¹,

Kinoshita²,

Itoh³

et al. 1995

FEBS Letters

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Phospholipase A2 (PLA2) from human pancreas, designated hPLAz-I, functions as a digestive enzyme. Interestingly, the present study demonstrated that the mature form of hPLA2-I stimulated the growth of a human pancreatic cancer cell line MIAPaCa-2, whereas the pro-form was ineffective. PLA2s from Laticauda semifasciata fraction I, Crotalus adamanteus venom, Streptomyces violaceoruber and bee venom, showed no proliferative effect to the growth of MIAPaCa-2. The Scatchard plot analysis revealed that the MIAPaCa-2 cell had a specific binding site for the mature hPLA2-I. The equilibrium binding constant (Kd) and the maximum binding capacity (Bmax) were 2.6 nM and 0.4 fmol/10 6 cells, respectively. These results suggest that the mature hPLA2-I, but not the pro-form, may function as a growth factor of pancreas carcinoma via the specific binding site.

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Section: Purification Of Hpla2-i From Human Pancreatic Juicesupporting

confidence: 79%

Human pancreatic phospholipase A₂ stimulates the growth of human pancreatic cancer cell line

Hanada¹,

Kinoshita²,

Itoh³

et al. 1995

FEBS Letters

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“…This could be achieved, in particular, by sitedirected mutagenesis experiments since an increasing number of cDNAs encoding phospholipases A2 originating from snakes venoms [40, 411 and mammalian pancreas [42] have been cloned and more recently expressed [43 ~ 471.…”

Section: Discussionmentioning

confidence: 99%

Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin

Mollier¹,

Chwetzoff²,

Bouet³

et al. 1989

European Journal of Biochemistry

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We prepared two derivatives of notexin, a phospholipase A2 from Motechis scutatus scutatus venom, by modifying the protein with 2-nitrophenylsulfenylchloride, a tryptophan-specific reagent. One derivative was modified at both tryptophans 20 and 110 whereas the other was modified at tryptophan 20. Evidence based on circular dichroic analysis and antigenicity towards a notexin-specific monoclonal antibody indicated that derivatization at both tryptophans did not affect the tertiary structure of notexin. Concomitant modification of tryptophans 20 and 110 induced a marked decrease in the capacity of notexin to kill mice and to block neuromuscular transmission in the chick biventer cervicis preparation, whereas selective modification at tryptophan 20 had no effect on the lethal properties of notexin. This implies that the decrease in the lethal properties of notexin after derivatization was due to modification at tryptophan 110. However, the diderivatized notexin retained full enzymatic activity, implying that neither tryptophan 20 and tryptophan 110 are involved in the catalytic function of the molecule. We conclude that notexin harbours two functional sites. One of them corresponds to the enzymatic site, whereas the other, which includes tryptophan 110, provides specific toxic characteristics to notexin. By reference to previous crystallographic studies, the relative spatial positions of elements involved in toxicity and the catalytic site, we propose a possible orientation of notexin with respect to its putative membrane-bound target.

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“…The reverse transcripton (RT) reaction mixture of 20 l contained 50 mM Tris-HCl (pH 8.2), 6 mM MgCl 2 , 10 mM DTT, 100 mM NaCl, 200 M dNTPs, 11 U RNAse inhibitor, 10 pmol primer (3 Ј primer of the corresponding cDNA: positions 695-719 for group II PLA 2 cDNA [25], 335-359 for group I PLA 2 [26], 978-1007 for annexin-I [27], and 980-1004 for GAPDH [28] from Microsynth GmbH, Balgach, Switzerland), 2-5 g of total RNA and 1 U of avian myeloblastosis virus reverse transcriptase (Boehringer Mannheim Biochemicals, Rotkreuz, Switzerland). For competitive RT-PCR 18 fg of modified group II PLA 2 transcript was added to the reverse transcription reaction (29).…”

Section: Methodsmentioning

confidence: 99%

Liver cirrhosis induces renal and liver phospholipase A2 activity in rats.

Vishwanath¹,

Frey²,

Escher³

et al. 1996

J. Clin. Invest.

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Maintenance of renal function in liver cirrhosis requires increased synthesis of arachidonic acid derived prostaglandin metabolites. Arachidonate metabolites have been reported to be involved in modulation of liver damage. The purpose of the present study was to establish whether the first enzyme of the prostaglandin cascade synthesis, the phospholipase A 2 (PLA 2 ) is altered in liver cirrhosis induced by bile duct excision. the mRNA of PLA 2 (group I and II) and annexin-I a presumptive inhibitor of PLA 2 enzyme was measured by PCR using glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an internal standard. The mean mRNA ratio of group II PLA 2 /GAPDH was increased in liver tissue by 126% ( P Ͻ 0.001) and in kidney tissue by 263% ( P Ͻ 0.006) following induction of liver cirrhosis. The increase in group II PLA 2 mRNA in cirrhotic animals was reflected by an increase in PLA 2 protein and enzyme activity in both liver and kidney tissues. Since the mRNA of group I PLA 2 was not detectable and Group IV PLA 2 activity measured in liver and kidney tissue samples was very low and not changed following induction of cirrhosis, it is likely that the major PLA 2 activity measured in liver and kidney corresponds to group II PLA 2 enzyme. The mean mRNA ratio of annexin-I/GAPDH was increased in liver tissue by 115% ( P Ͻ 0.05) but unchanged in kidney tissue following induction of cirrhosis. The protein content of annexin-I and -V were not affected by bile duct excision in liver and kidney tissue indicating that upregulation of group II PLA 2 activity was not due to downregulation of annexin-I or -V. Group II PLA 2 activity of glomerular mesangial cells stimulated by interleukin-1 ␤ was enhanced by bile juice and various bile salts. In conclusion, activity of group II PLA 2 is upregulated partly due to enhanced transcription and translation in cirrhosis and is furthermore augmented by elevated levels of bile salts. ( J. Clin. Invest. 1996. 98:365-371.)

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Dog and Rat Pancreatic Phospholipases A2: Complete Amino Acid Sequences Deduced from Complementary DNAs

Cited by 94 publications

References 0 publications

Human pancreatic phospholipase A₂ stimulates the growth of human pancreatic cancer cell line

Human pancreatic phospholipase A₂ stimulates the growth of human pancreatic cancer cell line

Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin

Liver cirrhosis induces renal and liver phospholipase A2 activity in rats.

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Dog and Rat Pancreatic Phospholipases A2: Complete Amino Acid Sequences Deduced from Complementary DNAs

Cited by 94 publications

References 0 publications

Human pancreatic phospholipase A2 stimulates the growth of human pancreatic cancer cell line

Human pancreatic phospholipase A2 stimulates the growth of human pancreatic cancer cell line

Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin

Liver cirrhosis induces renal and liver phospholipase A2 activity in rats.

Contact Info

Product

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Human pancreatic phospholipase A₂ stimulates the growth of human pancreatic cancer cell line

Human pancreatic phospholipase A₂ stimulates the growth of human pancreatic cancer cell line