tailieunhanh - Báo cáo Y học: Structural and biochemical characterization of calhepatin, an S100-like calcium-binding protein from the liver of lungfish (Lepidosiren paradoxa)

We report the biochemical characterization of calhepatin, a calcium-binding protein of the S100 family, isolated from lungfish (Lepidosiren paradoxa) liver. The primary structure, determined by Edman degradation and MS/MS, shows that the sequence identities with the other members of the family are lower than those between S100 proteins from different species. Calhepatin is composed of 75 residues and has a molecular mass of 8670 Da. It is smaller than calbindin D9k (78 residues), the smallest S100 described so far | Eur. J. Biochem. 269 3433-3441 2002 FEBS 2002 doi Structural and biochemical characterization of calhepatin an S100-like calcium-binding protein from the liver of lungfish Lepidosiren paradoxa Santiago M. Di Pietro and Jose A. Santome Instituto de Quimica y Fisicoquimica Biologicas IQUIFIB Facultad de Farmacia y Bioquimica Universidad de Buenos Aires Argentina We report the biochemical characterization of calhepatin a calcium-binding protein of the S100 family isolated from lungfish Lepidosiren paradoxa liver. The primary structure determined by Edman degradation and MS MS shows that the sequence identities with the other members of the family are lower than those between S100 proteins from different species. Calhepatin is composed of 75 residues and has a molecular mass of 8670 Da. It is smaller than calbindin D9k 78 residues the smallest S100 described so far. Sequence analysis and molecular modelling predict the two EF-hand motifs characteristic of the S100 family. Metal-binding properties were studied by a direct 45Ca2 -binding assay and by fluorescence titration. Calhepatin binds Ca2 and Cu2 but not Zn2 . Cu2 binding does not change the affinity of calhepatin for Ca2 . Calhepatin undergoes a conformational change upon Ca2 binding as shown by the increase in its intrinsic fluorescence intensity and kmax the decrease in the apo-calhepatin hydrodynamic volume and the Ca2 -dependent binding of the protein to phenyl-Superose. Like most S100 proteins calhepatin tends to form noncova-lently associated dimers. These data suggest that calhepatin is probably involved in Ca2 -signal transduction. Keywords calcium-binding protein EF-hand liver lungfish S100. Cytoplasmic Ca2 is a ubiquitous second messenger. The rise in intracellular Ca2 is a widely established signal controlling a variety of processes in eukaryotic cells such as cell growth and differentiation cell motility muscle contraction gene expression secretion nerve impulse .

• Báo cáo khoa học
• Traditional medicine
• Report medicine
• scientific reports
• breast cancer
• medicine
• chemical reaction
• Commercial use
• Tadehagi triquetrum (L ) H Ohashi
• Indigenous medicine in Myanmar
• Medicinal plants
• Calotropis gigantea R
• Br
• Traditional medicinal plants
• Local development in Myanmar
• Important role in health care system
• BMC Chemistry
• Trace analysis
• Dispersive solvent
• Traditional Chinese medicine
• Chinese medicine oral liquid
• Veterinary Medicine
• Herbal Medicine
• Varughese George
• Andrographis paniculata
• Chemical Constituents
• alternative medicine
• diagnostic techniques
• Diagnostic therapies
• Chinese medicine
• Medical herbalism
• Massage therapy review
• Lecture Massage therapy review
• Bodywork assessment
• Massage therapy
• Traditional chinese medicine modality
• Acanthospermum hispidum
• Burkina faso
• Pharmacognosic characterization
• Acanthospermum hispidum (Asteraceae)
• Medicinal plant widely
• Active components
• Plasma protein binding
• Research methods
• Doctoral thesis abstract
• Improving accounting work organization
• Accounting work organization
• Traditional medicine hospitals
• Hanoi city
• Vietnamese traditional medicine
• Medicinal herbs
• Ethnic groups
• Community healthcare
• Mountainous area
• Cultural Perspective
• Modern Medicine
• Funding Perspective
• Traditional Oriental
• cell proliferation
• oxidation
• gastric cancer
• hormone medicine
• tumor cells
• biochemical studies
• environmental medicine
• Crystal structure