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Biomedical subjects

C Arana

Publications and source records attributed to C Arana.

9 recordsLinked to original sources
PubMed2005

Hereditary blood coagulation disorders: management and dental treatment.

Patients with hereditary hemostatic disorders, characterized by a tendency to bleeding or thrombosis, constitute a serious challenge in the dental practice. Advances in the medical diagnosis of hemostatic disorders have exposed dental professionals to new patients not amenable to the application of the management protocols associated with other, more well-known, disorders. It is the aim of this paper to review the evidence, to highlight the areas of major concern, and to suggest management regimens for patients with hereditary hemostatic disorders. An extensive review has been made (PubMed, Science Direct, Web of Knowledge, etc.) of literature pertaining to hereditary disorders affecting blood coagulation factors and how they affect the practice of dentistry. Several aspects relating to the care of such patients must be recognized and taken into consideration when dental treatment is planned. Replacement of deficient coagulation factors ensures that safe dental treatment will be carried out. However, the half-life of such coagulation factors requires that dental treatment be specifically planned and adapted to the type of pathology involved.

Blood Coagulation Disorders, Inherited↗
PubMed2000

Familial hypertrophic cardiomyopathy mutations in the regulatory light chains of myosin affect their structure, Ca2+ binding, and phosphorylation.

The effect of the familial hypertrophic cardiomyopathy mutations, A13T, F18L, E22K, R58Q, and P95A, found in the regulatory light chains of human cardiac myosin has been investigated. The results demonstrate that E22K and R58Q, located in the immediate extension of the helices flanking the regulatory light chain Ca(2+) binding site, had dramatically altered Ca(2+) binding properties. The K(Ca) value for E22K was decreased by approximately 17-fold compared with the wild-type light chain, and the R58Q mutant did not bind Ca(2+). Interestingly, Ca(2+) binding to the R58Q mutant was restored upon phosphorylation, whereas the E22K mutant could not be phosphorylated. In addition, the alpha-helical content of phosphorylated R58Q greatly increased with Ca(2+) binding. The A13T mutation, located near the phosphorylation site (Ser-15) of the human cardiac regulatory light chain, had 3-fold lower K(Ca) than wild-type light chain, whereas phosphorylation of this mutant increased the Ca(2+) affinity 6-fold. Whereas phosphorylation of wild-type light chain decreased its Ca(2+) affinity, the opposite was true for A13T. The alpha-helical content of the A13T mutant returned to the level of wild-type light chain upon phosphorylation. The phosphorylation and Ca(2+) binding properties of the regulatory light chain of human cardiac myosin are important for physiological function, and alteration any of these could contribute to the development of hypertrophic cardiomyopathy.

Amino Acid Sequence↗
PubMed1994

[Bacteremia and recurrent arthritis caused by Streptococcus pyogenes in a heroin addict with AIDS].

BACKGROUND: Streptococcus pyogenes is a bacteria which, at present, is seldom isolated in blood and articular fluid. An intravenous drug addict with human immunodeficiency virus infection, with bacteremia and arthritis by S. pyogenes, associated with tuberculosis is presented. METHODS: Blood and articular fluid cultures were collected in the usual and Löwenstein-Jensen media. RESULTS: The patient improved with penicillin and tuberculostatic drugs. Nine months after this episode, the patient reinitiated intravenous drug addiction, and developed another presentation of bacteremia and arthritis by S. pyogenes. CONCLUSIONS: Heroin addict patients constitute a risk group for bacteremias ans severe infections by S. pyogenes.

Acquired Immunodeficiency Syndrome↗