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Article: A confidential online grade posting system: student scores on the Internet.

Thielke, S M / Vincenzi, F F

Proceedings of the Western Pharmacology Society

2001 Volume 44, Page(s) 133–134

MeSH term(s)	Computer Security ; Education, Pharmacy/methods ; Internet ; Students, Pharmacy ; Teaching
Language	English
Publishing date	2001
Publishing country	United States
Document type	Journal Article
ZDB-ID	603499-8
ISSN	0083-8969
ISSN	0083-8969
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Article: Stobadine: bellwether of a broader view of drug actions.

Vincenzi, F F / Hinds, T R

Life sciences

1999 Volume 65, Issue 18-19, Page(s) 1857–1864

Abstract: Stobadine was recognized early in its development as having antioxidant properties. A number of laboratories found associations between the antioxidant properties of stobadine and its potential beneficial effects. We found that stobadine acted as an ... ...

Abstract	Stobadine was recognized early in its development as having antioxidant properties. A number of laboratories found associations between the antioxidant properties of stobadine and its potential beneficial effects. We found that stobadine acted as an antioxidant in a modification of an oxygen radical absorbance capacity (ORAC) assay. Similar results were observed with other drugs, including tirilazad and pramipexole. We suggest that stobadine and certain other drugs exhibit antioxidant properties in both hydrophilic and hydrophobic environments. Other drugs have been developed for their antioxidant properties and some currently marketed drugs have antioxidant properties. Although they may not have been explicitly sought during development, at least some of the beneficial effects may be related to antioxidant properties and/or scavenging of free radicals. Because stobadine was one of the first drugs for which useful properties were associated with its antioxidant actions, stobadine may be seen as a bellwether of a broader view of pharmacological actions--a view that encompasses antioxidant properties as a useful basis of therapeutic effects.
MeSH term(s)	Antioxidants/chemistry ; Carbolines/chemistry ; Free Radical Scavengers/chemistry ; Phycoerythrin/chemistry ; Water/chemistry
Chemical Substances	Antioxidants ; Carbolines ; Free Radical Scavengers ; Water (059QF0KO0R) ; Phycoerythrin (11016-17-4) ; dicarbine (Y0EA50IJ3V)
Language	English
Publishing date	1999
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/s0024-3205(99)00438-5
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Article: Pramipexole has antioxidant properties and inhibits lipid peroxidation.

Vincenzi, F F / Hinds, T R

Proceedings of the Western Pharmacology Society

1998 Volume 41, Page(s) 43–46

MeSH term(s)	Benzothiazoles ; Dose-Response Relationship, Drug ; Free Radical Scavengers/pharmacology ; In Vitro Techniques ; Lipid Peroxidation/drug effects ; Photolysis ; Temperature ; Thiazoles/pharmacology
Chemical Substances	Benzothiazoles ; Free Radical Scavengers ; Thiazoles ; pramipexole (83619PEU5T)
Language	English
Publishing date	1998
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603499-8
ISSN	0083-8969
ISSN	0083-8969
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Article: Pharmacological modification of the Ca2+-pump ATPase activity of human erythrocytes.

Vincenzi, F F

Annals of the New York Academy of Sciences

1982 Volume 402, Page(s) 368–380

Abstract: The Ca2+-pump ATPase of human RBC membranes appears to be exquisitely sensitive to a variety of amphipathic molecules. The acidic protein calmodulin (CaM) activates the enzyme some three- to fivefold with an apparent Kd of approximately 1-5 nM. A variety ...

Abstract	The Ca2+-pump ATPase of human RBC membranes appears to be exquisitely sensitive to a variety of amphipathic molecules. The acidic protein calmodulin (CaM) activates the enzyme some three- to fivefold with an apparent Kd of approximately 1-5 nM. A variety of other amphipathic anions, such as acidic phospholipids, free fatty acids, and anionic detergents, are less potent and in some cases less efficacious than CaM, but also activate the enzyme. Similar results have been observed for other CaM-dependent enzymes, and it is suggested that these agents mimic CaM in a general, but rather nonspecific, fashion. Activation of the human RBC Ca2+-pump ATPase by CaM or other amphipathic anions can be selectively antagonized by a wide variety (structurally and pharmacologically) of amphipathic cations. There is no simple relationship between antagonism of CaM in vitro and the general systemic pharmacology of these drugs. The only common feature of such drugs is that they are amphipathic cations. Neutral molecules such as saponin exerted neither CaM-like activity nor CaM antagonism. Great caution is urged in the inferential use of presumed anti-CaM drugs to study biological systems.
MeSH term(s)	Biological Transport, Active ; Ca(2+) Mg(2+)-ATPase ; Calcium/blood ; Calcium-Transporting ATPases/blood ; Calmodulin/pharmacology ; Emetine/pharmacology ; Enzyme Activation ; Erythrocyte Membrane/enzymology ; Erythrocytes/enzymology ; Humans ; Kinetics ; Saponins/pharmacology
Chemical Substances	Calmodulin ; Saponins ; Ca(2+) Mg(2+)-ATPase (EC 3.6.1.-) ; Calcium-Transporting ATPases (EC 3.6.3.8) ; Calcium (SY7Q814VUP) ; Emetine (X8D5EPO80M)
Language	English
Publishing date	1982
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	211003-9
ISSN	1749-6632 ; 0077-8923
ISSN (online)	1749-6632
ISSN	0077-8923
DOI	10.1111/j.1749-6632.1982.tb25755.x
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Article: Red blood cell calmodulin and Ca2+ pump ATPase: preliminary results of a species comparison.

Vincenzi, F F

Progress in clinical and biological research

1981 Volume 55, Page(s) 363–383

Abstract: Membrane-bound ATPases of the red blood cells from five mammalian species were compared. Large differences were observed in the specific activities of (Mg2+)-ATPase, (Na++K+Mg2+)-ATPase and (Ca2+/Mg2+)-ATPase. by contrast, calmodulin activities of red ... ...

Abstract	Membrane-bound ATPases of the red blood cells from five mammalian species were compared. Large differences were observed in the specific activities of (Mg2+)-ATPase, (Na++K+Mg2+)-ATPase and (Ca2+/Mg2+)-ATPase. by contrast, calmodulin activities of red blood cell lysates from the five species were similar. Results are considered in light of possible mechanisms for regulation of Na+ and Ca2+ in red blood cells.
MeSH term(s)	Adenosine Triphosphatases/blood ; Animals ; Biological Transport, Active ; Ca(2+) Mg(2+)-ATPase ; Calcium/blood ; Calcium-Binding Proteins/blood ; Calcium-Transporting ATPases/blood ; Calmodulin/blood ; Dogs ; Enzyme Activation ; Erythrocyte Membrane/metabolism ; Erythrocytes/metabolism ; Goats ; Humans ; Rabbits ; Sheep ; Sodium-Potassium-Exchanging ATPase/blood ; Species Specificity
Chemical Substances	Calcium-Binding Proteins ; Calmodulin ; Adenosine Triphosphatases (EC 3.6.1.-) ; Ca(2+) Mg(2+)-ATPase (EC 3.6.1.-) ; magnesium sodium potassium ATPase (EC 3.6.1.-) ; Calcium-Transporting ATPases (EC 3.6.3.8) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	1981
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ISSN	0361-7742
ISSN	0361-7742
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Pharmacological differentiation of calmodulin receptors?

Vincenzi, F F

Proceedings of the Western Pharmacology Society

1981 Volume 24, Page(s) 193–196

MeSH term(s)	Adenosine Triphosphatases/metabolism ; Ca(2+) Mg(2+)-ATPase ; Calcium-Binding Proteins/metabolism ; Calcium-Transporting ATPases/metabolism ; Calmodulin/metabolism ; Erythrocyte Membrane/enzymology ; Humans ; In Vitro Techniques ; Receptors, Cell Surface/metabolism ; Sodium-Potassium-Exchanging ATPase/metabolism
Chemical Substances	Calcium-Binding Proteins ; Calmodulin ; Receptors, Cell Surface ; Adenosine Triphosphatases (EC 3.6.1.-) ; Ca(2+) Mg(2+)-ATPase (EC 3.6.1.-) ; Calcium-Transporting ATPases (EC 3.6.3.8) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
Language	English
Publishing date	1981
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	603499-8
ISSN	0083-8969
ISSN	0083-8969
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Article: Calmodulin pharmacology.

Vincenzi, F F

Cell calcium

1981 Volume 2, Issue 4, Page(s) 387–409

Abstract: Calmodulin (CaM) is a major intracellular receptor for Ca2+. CaM is thus a crucial receptor to consider in pharmacological modification of cellular activity. Potential mechanisms by which drugs may modify CaM effectiveness are considered in the context ... ...

Abstract	Calmodulin (CaM) is a major intracellular receptor for Ca2+. CaM is thus a crucial receptor to consider in pharmacological modification of cellular activity. Potential mechanisms by which drugs may modify CaM effectiveness are considered in the context of its interaction with Ca2+ and in turn with its various effectors. Some examples of established drug mechanisms are considered. A wide range of chemical compounds representing diverse pharmacological classes are anti-CaM under some conditions. No simple relationships have been established between molecular level events and therapeutic applicability of anti-CaM compounds.
MeSH term(s)	Calcium/antagonists & inhibitors ; Calcium/metabolism ; Calcium-Binding Proteins/antagonists & inhibitors ; Calmodulin/analysis ; Calmodulin/antagonists & inhibitors ; Calmodulin/physiology ; Calmodulin-Binding Proteins ; Carrier Proteins/metabolism ; Humans ; Psychotropic Drugs/metabolism ; Receptors, Drug/drug effects
Chemical Substances	Calcium-Binding Proteins ; Calmodulin ; Calmodulin-Binding Proteins ; Carrier Proteins ; Psychotropic Drugs ; Receptors, Drug ; Calcium (SY7Q814VUP)
Language	English
Publishing date	1981-08
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/0143-4160(81)90027-0
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Article: Calmodulin in the regulation of intracellular calcium.

Vincenzi, F F

Proceedings of the Western Pharmacology Society

1979 Volume 22, Page(s) 289–294

MeSH term(s)	Animals ; Biological Transport, Active ; Calcium/metabolism ; Calcium-Binding Proteins/physiology ; Calcium-Transporting ATPases/metabolism ; Calmodulin/physiology ; Erythrocyte Membrane/metabolism
Chemical Substances	Calcium-Binding Proteins ; Calmodulin ; Calcium-Transporting ATPases (EC 3.6.3.8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	1979
Publishing country	United States
Document type	Journal Article
ZDB-ID	603499-8
ISSN	0083-8969
ISSN	0083-8969
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Article: Regulation of a plasma membrane calcium pump: a speculative model.

Vincenzi, F F

Annals of the New York Academy of Sciences

1978 Volume 307, Page(s) 229–231

MeSH term(s)	Animals ; Biological Transport, Active ; Blood Proteins/metabolism ; Calcium/metabolism ; Carrier Proteins/metabolism ; Cyclic AMP/metabolism ; Cytoplasm/metabolism ; Erythrocyte Membrane/metabolism ; Erythrocytes/metabolism ; In Vitro Techniques ; Models, Biological
Chemical Substances	Blood Proteins ; Carrier Proteins ; Cyclic AMP (E0399OZS9N) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	1978-04-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	211003-9
ISSN	1749-6632 ; 0077-8923
ISSN (online)	1749-6632
ISSN	0077-8923
DOI	10.1111/j.1749-6632.1978.tb41949.x
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Article: Numerical simulation of assay of the calcium pump of intact red blood cells.

Vincenzi, F F / Hinds, T R

Biochimica et biophysica acta

1992 Volume 1106, Issue 1, Page(s) 63–70

Abstract: An assay of the Ca pump ATPase of intact human RBCs is described in a companion paper (Wu, L., Hinds, T. R. and Vincenzi, F. F. (1992) Biochim. Biophys. Acta 1106, 56-62). The assay is based on the rapid loss of ATP in RBCs that occurs when the cells are ...

Abstract	An assay of the Ca pump ATPase of intact human RBCs is described in a companion paper (Wu, L., Hinds, T. R. and Vincenzi, F. F. (1992) Biochim. Biophys. Acta 1106, 56-62). The assay is based on the rapid loss of ATP in RBCs that occurs when the cells are exposed to the ionophore, A23187, in the presence of Ca. An unexpected finding was that the initial loss of ATP follows pseudo-first-order kinetics. This was unexpected because the ATP content of RBCs is somewhat higher than the Km of the Ca pump for ATP. Thus, the initial loss of ATP would be expected to follow zero-order kinetics; at least if the Ca pump ATPase operated with Michaelis kinetics. We performed a series of computer simulations of the Ca pump ATPase to investigate the possible cause of the unexpected pseudo-first-order behavior. The results confirmed that the data can not be accounted for by Michaelis kinetics of the Ca pump ATPase. Possible effects of adenylate kinase were tested and were also not found to account for the pseudo-first-order behavior of an ATPase operating with Michaelis kinetics. The enzymatic properties of the Ca pump ATPase were re-examined. It was found that the Ca pump ATPase exhibits positive cooperativity toward ATP. The apparent cooperativity was 1.91. In simulations it was found that positive cooperativity of the Ca pump ATPase in the range of 1.5 to 2.0 could account for the pseudo-first-order behavior. Excellent fit of the simulation data to first-order behavior was true with or without any contribution from adenylate kinase. Rate constants of ATP loss were thus examined using cooperativity of 2.0. Over a wide range the rate constant of the loss of ATP was directly proportional to the assumed Vmax of the Ca pump ATPase, but only if the data were limited to loss of less than 67% of the initial ATP. It is suggested, therefore, that the rate constant for the initial loss of ATP in intact RBCs, as stimulated by the ionophore A23187, can be taken as a measure of the capacity of the Ca pump ATPase.
MeSH term(s)	Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Adenylate Kinase/metabolism ; Calcium-Transporting ATPases ; Enzyme Activation ; Erythrocytes/enzymology ; Erythrocytes/metabolism ; Humans ; Kinetics ; Models, Theoretical
Chemical Substances	Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Adenylate Kinase (EC 2.7.4.3) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	1992-04-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/0005-2736(92)90222-8
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