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1.
J Biol Regul Homeost Agents ; 31(2 Suppl 1): 147-154, 2017.
Article in English | MEDLINE | ID: mdl-28691466

ABSTRACT

Osteocartilagineous differentiation within malignant melanoma is a rare occurrence with several implications for diagnosis. Most of the reported cases have occurred in acral lentiginous malignant melanomas. In this paper, the authors describe the clinical, morphological, immunohistochemical features and surgical treatment of a case of primary oral mucosal melanoma with osteocartilaginous differentiation and they review the existing literature. The clinical history of a 67-year-old man affected of oral malignant melanoma was described from the first presentation to the second recurrence. FISH analysis on primary lesion and on relapses showed positive results both in epithelioid and in osteocondroblastic areas. Because of the scarcity of literature in osteogenic melanoma, histological identification may be problematic and prognostic factors and therapeutic protocols are nor well established. Immunohistochemical and molecular techniques can help to diagnosis this rare lesion.


Subject(s)
Melanoma/pathology , Skin Neoplasms/pathology , Aged , Cell Differentiation , Humans , Male , Melanoma/diagnosis , Mouth Mucosa/pathology , Skin Neoplasms/diagnosis
2.
Biosci Rep ; 21(1): 81-91, 2001 Feb.
Article in English | MEDLINE | ID: mdl-11508697

ABSTRACT

In order to gain some insight into mitochondria permeability under water stress, intact coupled mitochondria were isolated from water stress adapted potato cells and investigations were made of certain transport processes including the succinate/malate and ADP/ATP exchanges, the plant mitochondrial ATP-sensitive potassium channel (PmitoKATP) and the plant uncoupling mitochondrial protein (PUMP). The Vmax values measured for succinate/malate and ADP/ATP carriers, as photometrically investigated, as well as the same values for the PmitoK(ATP) and the PUMP were found to increase; this suggested that mitochondria adaptation to water stress can cause an increase in the membrane permeability.


Subject(s)
Energy Metabolism/physiology , Intracellular Membranes/metabolism , Mitochondria/metabolism , Solanum tuberosum/metabolism , Water-Electrolyte Balance/physiology , Adenosine Diphosphate/metabolism , Adenosine Triphosphate/metabolism , Carrier Proteins/drug effects , Carrier Proteins/metabolism , Energy Metabolism/drug effects , Intracellular Membranes/drug effects , Ion Channels , Malates/metabolism , Membrane Proteins/drug effects , Membrane Proteins/metabolism , Mitochondria/drug effects , Mitochondrial ADP, ATP Translocases/drug effects , Mitochondrial ADP, ATP Translocases/metabolism , Mitochondrial Proteins , Models, Biological , Permeability , Potassium Channels/drug effects , Potassium Channels/metabolism , Solanum tuberosum/cytology , Solanum tuberosum/drug effects , Succinic Acid/metabolism , Uncoupling Protein 1 , Water-Electrolyte Balance/drug effects
3.
FEBS Lett ; 462(3): 313-6, 1999 Dec 03.
Article in English | MEDLINE | ID: mdl-10622717

ABSTRACT

In this study, we investigated the metabolite permeability of isolated coupled Saccharomyces cerevisiae mitochondria. The occurrence of a fumarate/malate antiporter activity was shown. The activity differs from that of the dicarboxylate carrier (which catalyses the succinate/malate antiport) in (a) kinetics (Km and Vmax values are about 27 microM and 22 nmol min(-1) mg protein(-1) and 70 microM and 4 nmol min(-1) mg protein(-1), respectively), (b) sensitivity to inhibitors, (c) Ki for the competitive inhibitor phenylsuccinate and (d) pH profiles.


Subject(s)
Antiporters/metabolism , Fumarates/metabolism , Malates/metabolism , Mitochondria/metabolism , Saccharomyces cerevisiae/metabolism , Succinates/metabolism , Adenosine Diphosphate/metabolism , Adenosine Triphosphate/metabolism , Antiporters/antagonists & inhibitors , Biological Transport, Active , Hydrogen-Ion Concentration , Kinetics , Saccharomyces cerevisiae/ultrastructure
4.
FEBS Lett ; 428(3): 245-9, 1998 May 29.
Article in English | MEDLINE | ID: mdl-9654142

ABSTRACT

Evidence is given that mitochondria isolated from Saccharomyces cerevisiae can take up externally added riboflavin and synthesise from it both flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) probably due to the existence of the mitochondrial riboflavin kinase already reported and the novel mitochondria FAD synthetase. Moreover Saccharomyces cerevisiae mitochondria can export the newly synthesised flavin derivatives to the extramitochondrial phase. This has been proven to take place with 1:1 stoichiometry with riboflavin decrease outside mitochondria, thus showing that flavin traffic occurs across the mitochondrial membranes.


Subject(s)
Flavin Mononucleotide/metabolism , Flavin-Adenine Dinucleotide/metabolism , Mitochondria/metabolism , Riboflavin/metabolism , Saccharomyces cerevisiae/metabolism , Flavin Mononucleotide/biosynthesis , Flavin-Adenine Dinucleotide/biosynthesis , Kinetics , Nucleotidyltransferases/metabolism , Oxygen Consumption , Phosphotransferases (Alcohol Group Acceptor)/metabolism , Time Factors
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