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1.
J Subst Abuse Treat ; 21(3): 167-72, 2001 Oct.
Article in English | MEDLINE | ID: mdl-11728791

ABSTRACT

Alcohol screening of severely injured patients should be universal. Hospitalization following alcohol-related injury provides an opportunity for intervention to reduce recidivism. This study examines the frequency of social services referral of an alcohol positive cohort of adolescent trauma patients. This was a retrospective analysis of data collected from 1994 through 1998 by the National Pediatric Trauma Registry. All patients between the ages of 12 and 17 who had a blood alcohol level (BAL) measured were analyzed. Patients receiving referral to the department of social services, family counseling, or addiction services, and those receiving any substance abuse education intervention were considered a positive referral. There were 6006 children age 12 to 17 included in the database during this five-year period, 751 of whom had a BAL measured. Of those screened, 15.5% were positive. Sixty-eight (59%) of the BAL positive patients were referred for intervention through social services. The only statistically significant predictor of referral was whether or not the patient was the operator of a vehicle involved in the motor vehicle collision. Nearly half of the adolescents in this study, who screened positive for alcohol, received no social services support.


Subject(s)
Adolescent, Hospitalized/psychology , Alcoholic Intoxication/diagnosis , Referral and Consultation/statistics & numerical data , Social Work Department, Hospital , Wounds and Injuries/etiology , Accidents, Traffic , Adolescent , Alcoholic Intoxication/blood , Alcoholic Intoxication/complications , Female , Humans , Male , Mass Screening , New England/epidemiology , Registries , Retrospective Studies , Risk Factors , Trauma Severity Indices , Wounds and Injuries/epidemiology , Wounds and Injuries/rehabilitation
2.
Ann Emerg Med ; 34(6): 715-9, 1999 Dec.
Article in English | MEDLINE | ID: mdl-10577400

ABSTRACT

STUDY OBJECTIVE: Emergency department records are an important source of injury surveillance data. However, documentation regarding intentional assault has not been studied and may be suboptimal. The purpose of this study was to analyze physician documentation of assailant, site, and object used in intentional assault. METHODS: The ED log of an urban Level I trauma center was retrospectively reviewed to identify eligible patients presenting consecutively in November 1996. All acutely injured patients not involved in a motorized vehicle crash were identified. RESULTS: From the ED log, 1, 483 patients were identified as possible study subjects; 1,457 (98%) charts were located and reviewed and 971 (67%) met inclusion criteria. Of these, 288 (30%) cases resulted from intentional assault. In 67% of patients, there was no documentation of the identity of the assailant. For 13% of cases, there was no documentation regarding the object or force used in the assault. In 79% of cases there was no documentation regarding the site of assault. For 24 cases (8%), the assailant was documented as an intimate partner or ex-partner. Police involvement in these cases was documented 54% of the time, despite the fact that this state mandates police reports for cases of acute partner violence. Social service involvement and shelter referrals were documented in less than one fourth of domestic violence cases. CONCLUSION: Although the ED commonly treats patients who have been assaulted, basic surveillance data are often omitted from the chart. Structured charting may provide more complete data collection.


Subject(s)
Domestic Violence , Emergency Service, Hospital , Medical Records/standards , Colorado , Humans , Massachusetts , Retrospective Studies , Trauma Centers , Trauma Severity Indices , Urban Health
3.
Biol Reprod ; 61(4): 1042-9, 1999 Oct.
Article in English | MEDLINE | ID: mdl-10491642

ABSTRACT

The copper-binding protein, ceruloplasmin, is both a serum component and a secretory product of Sertoli cells. Studies on serum ceruloplasmin have demonstrated it to be a ferroxidase that is essential for iron transport throughout the body. We report here that a glycosyl phosphatidylinositol (GPI)-anchored form of ceruloplasmin is expressed by Sertoli cells. Sertoli cell GPI-anchored proteins were selectively released by phosphatidylinositol-specific phospholipase C and were analyzed by Western blotting. A 135-kDa band was identified as ceruloplasmin by multiple antibody recognition and by amino acid sequence analysis. The presence of the GPI anchor on ceruloplasmin was confirmed by Triton X-114 phase partitioning experiments and by recognition with an antibody to the GPI anchor. GPI-anchored ceruloplasmin was enriched in detergent-insoluble glycolipid-enriched membrane microdomains (DIGs) of Sertoli cells. This is the first report of GPI-anchored ceruloplasmin in Sertoli cells and the first study of GPI-anchored ceruloplasmin in DIGs. We suggest that GPI-anchored ceruloplasmin may be the dominant form expressed by Sertoli cells and that Sertoli cell DIGs may play a role in iron metabolism within the seminiferous tubule.


Subject(s)
Cell Adhesion , Ceruloplasmin/metabolism , Detergents/pharmacology , Glycosylphosphatidylinositols/metabolism , Sertoli Cells/metabolism , Animals , Blotting, Western , Cells, Cultured , Electrophoresis, Polyacrylamide Gel , Male , Rats , Rats, Sprague-Dawley , Solubility , Type C Phospholipases/metabolism
4.
Biochem Cell Biol ; 70(6): 496-503, 1992 Jun.
Article in English | MEDLINE | ID: mdl-1333233

ABSTRACT

The relative contribution of the Sertoli cell and the pachytene spermatocyte to dolichol and N-linked oligosaccharide biosynthesis within the seminiferous tubule was investigated. Evidence is presented to show that the interaction between these two cell types affects dolichol and N-linked oligosaccharide biosynthesis. Analysis of the dolichol content of Sertoli cultures confirms earlier data suggesting that the Sertoli cell constitutes the major pool of dolichols within the seminiferous tubule. [14C]Acetate incorporation studies suggest that the Sertoli cell in culture synthesizes dolichol much more rapidly than does the isolated pachytene spermatocyte. This information, in addition to previous data in the literature, infers an interactive effect whereby the presence of the spermatogenic cell in the tubule stimulates dolichol synthesis in the Sertoli cell. The absence of normal Sertoli-spermatocyte interactions in in vitro incubations may also limit dolichol synthesis in the pachytene spermatocyte. The distribution of dolichol kinase between the Sertoli and the pachytene spermatocyte was also examined. The concentration of this enzyme in the Sertoli cell suggests the presence of an active salvage pathway within that cell. The correlation between the appearance of the pachytene spermatocyte and the previously described peak of dolichol kinase activity in the seminiferous tubules of the prepubertal animal implies cell-cell interactions. Radiolabelling studies of N-linked oligosaccharides were conducted using [3H]mannose and concanavalin A affinity chromatography to identify multiantennary, biantennary, and high-mannose oligosaccharide pools. An in vitro bicameral coculture system was used to demonstrate that pachytene spermatocytes stimulate incorporation of [3H]mannose into Sertoli cell oligosaccharides.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Dolichols/metabolism , Oligosaccharides/biosynthesis , Phosphotransferases (Alcohol Group Acceptor) , Testis/metabolism , Animals , Cell Communication , Dolichol Phosphates/metabolism , Glycopeptides/metabolism , Male , Phosphotransferases/metabolism , Rats , Rats, Sprague-Dawley , Seminiferous Tubules/cytology , Seminiferous Tubules/metabolism , Sertoli Cells/metabolism , Spermatocytes/metabolism
5.
Biol Reprod ; 43(4): 659-64, 1990 Oct.
Article in English | MEDLINE | ID: mdl-2126965

ABSTRACT

This study evaluated the responsiveness of Sertoli cell glycosylation in vitro to changes in culture age and to the presence of a reconstituted basement membrane (Matrigel) or collagen IV/laminin substrata. Primary Sertoli cell cultures were prepared from 20-day-old rats and incubated with [3H]mannose, a monosaccharide specific for asparagine-linked oligosaccharides. The cells were harvested on Days 4, 6, or 10 of culture life. A supernatant enriched in cell-surface glycopeptides (the trypsinate) and a cell pellet stripped of surface glycoconjugates were evaluated separately. Glycopeptides derived from a Pronase digest of the two samples were fractionated using concanavalin-A lectin affinity chromatography into three major classes: multiantennary complex-type, biantennary complex-type, and high-mannose-type oligosaccharide structures. The proportion of radiolabeled glycopeptides appearing in each of the three classes did not differ between Days 4 and 6 of culture. In contrast, a significant increase in the percentage of radiolabeled glycopeptides containing multiantennary complex-type oligosaccharides was observed in cells harvested from the 10-day-old cultures. In other experiments, Sertoli cells were grown on various substrata: plastic; collagen IV/laminin; or Matrigel, a reconstituted basement membrane (RBM) composed of laminin, collagen IV, proteoglycan sulfate, entactin, and nidogen. Growth on RBM significantly increased multiantennary complex-type oligosaccharide formation compared to plastic, whereas the high-mannose-type glycopeptides increased in cells grown on collagen IV/laminin. These studies suggest that environmental and physiological conditions such as culture age and the presence of extracellular matrix significantly affect glycosylation patterns in Sertoli cell cultures.


Subject(s)
Aging/metabolism , Extracellular Matrix/physiology , Membrane Glycoproteins , Sertoli Cells/metabolism , Aging/physiology , Animals , Cells, Cultured , Collagen/pharmacology , Culture Media/pharmacology , Drug Combinations , Glycosylation , Laminin/pharmacology , Male , Membrane Proteins/pharmacology , Plastics/pharmacology , Proteoglycans/pharmacology , Rats , Rats, Inbred Strains , Sertoli Cells/drug effects , Sertoli Cells/physiology
6.
Biol Reprod ; 34(3): 518-26, 1986 Apr.
Article in English | MEDLINE | ID: mdl-3008868

ABSTRACT

Dolichyl phosphate concentrations, a primary factor in regulating the rate of N-glycosidically linked glycoprotein synthesis, are dependent upon a cytidine triphosphate (CTP)-dependent dolichol kinase. This study examines dolichol kinase in rat testicular microsomes and defines assay conditions. As with dolichol kinases from other tissues, addition of 2-mercaptoethanol increased activity 60%. Inclusion of NaF, an inhibitor of testicular dolichyl phosphate phosphatase activity, also resulted in a 38% increase in activity. Triton X-100 was necessary for phosphorylation of both endogenous and exogenous dolichol; however, concentrations of detergent in excess of 0.25-0.35% were inhibitory. A 2- to 5-fold stimulation of kinase activity was obtained by addition of 50-100 microM exogenous dolichol. The high level of nucleoside triphosphatase activity in testicular microsomes mandated the inclusion of high levels of uridine triphosphate (UTP) to protect the [gamma-32 P] CTP. Increasing UTP concentrations up to 50 mM resulted in increased product formation. A clear requirement for divalent cations was observed; 5 mM ethylenediaminetetraacetate (EDTA) abolished activity. The following order of cation effectiveness was observed: Mn greater than or equal to Ca greater than Cd greater than Zn much greater than Mg. Ten mM optima were established for Ca2+ and Mn2+; the presence of UTP, however, results in significantly reduced concentrations of free Ca2+. Ion combination studies demonstrated interactive inhibitory effects between Ca2+ and other stimulatory divalent cations. Addition of 2 microM brain calmodulin, in the presence of 10 mM Ca2+, resulted in a 75-100% stimulation of activity.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Phosphotransferases (Alcohol Group Acceptor) , Phosphotransferases/metabolism , Testis/enzymology , Age Factors , Animals , Calcium/pharmacology , Calmodulin/antagonists & inhibitors , Calmodulin/pharmacology , Cations/pharmacology , Cytidine Triphosphate/metabolism , Dolichols/pharmacology , Fluorides/pharmacology , Male , Microsomes/enzymology , Rats , Testis/growth & development , Uridine Triphosphate/pharmacology
7.
Biol Reprod ; 34(1): 89-95, 1986 Feb.
Article in English | MEDLINE | ID: mdl-3955142

ABSTRACT

Dolichols, linear isoprenoids essential in the biosynthesis of N-glycosylated glycoproteins, are abundant in testicular tissue. This study investigated the distribution of dolichols among testicular cell and subcellular fractions. In addition, the accumulation of dolichol within the rat testis as a function of age was investigated. Dolichol content expressed either as total dolichol/testicle or as dolichol/mg protein exhibited a marked and continuous increase between 14 and 60 days of age. The 4-, 6-, 9-, and 12-mo-old animals exhibited only minor increases in testicular dolichol content. Mean value for retired breeders was 279 ng dolichol/mg protein. Although previous studies have suggested that dolichol synthesis occurs primarily within the spermatogenic cell, elutriation-purified spermatogenic cell fractions showed very low concentrations of dolichol. Pachytene spermatocyte and round spermatid fractions contained 25.8 and 36.5 ng dolichol/mg protein, respectively. Washed epididymal sperm also had a very low dolichol content (18.8 ng dolichol/mg protein). Recovery studies during elutriation purification of spermatogenic cells showed that the majority of dolichol was contained within the Sertoli-rich tubular fragments. Microsomal fractions isolated from whole testis exhibited a small enrichment (1.6-fold) in dolichol content, whereas Golgi apparatus fractions exhibited a large (12-fold) enrichment over that of the initial homogenate. These studies suggest that, although dolichols may be synthesized within the spermatogenic cell, they accumulate within the Sertoli cell.


Subject(s)
Diterpenes/analysis , Dolichols/analysis , Testis/growth & development , Aging , Animals , Chromatography, High Pressure Liquid , Epididymis , Male , Microsomes/analysis , Rats , Rats, Inbred Strains , Spermatozoa/analysis , Subcellular Fractions/analysis
8.
J Hand Surg Am ; 9(5): 707-10, 1984 Sep.
Article in English | MEDLINE | ID: mdl-6491216

ABSTRACT

Ten open radiocarpal fracture-dislocations in nine patients were treated by wound debridement, open reduction, and maintenance of reduction by casting supplemented with internal or external fixation. Eight patients had associated fractures or dislocations of the ipsilateral extremity: elbow fracture or dislocation (three patients), shoulder fracture (one patient), fractured humerus (two patients), and phalangeal fractures (three patients). In seven of ten cases the median and/or ulnar nerve was severely contused and required immediate decompression. Six patients were followed at least 15 months. All had mild asymptomatic sensory neurologic deficit, diminished range of motion of the wrist, and wrist pain with activity. The prognosis should be guarded.


Subject(s)
Carpal Bones/injuries , Fractures, Open/surgery , Joint Dislocations/surgery , Radius Fractures/surgery , Adult , Aged , Bone Nails , Bone Screws , Carpal Tunnel Syndrome/etiology , Casts, Surgical , Fracture Fixation , Fracture Fixation, Internal , Fractures, Open/complications , Humans , Male , Middle Aged
9.
Clin Nucl Med ; 8(2): 50-3, 1983 Feb.
Article in English | MEDLINE | ID: mdl-6825352

ABSTRACT

Bone scintigraphy is a very useful technique for detection of aseptic necrosis. We have used this diagnostic tool in a patient to detect aseptic necrosis of the talus, a common complication stemming from foot injuries. The scintigraphic pattern is rather typical and antedates any other radiographic changes. This technique appears to be very useful for diagnosis and follow-up of aseptic necrosis occurring during talar injuries.


Subject(s)
Diphosphonates , Osteonecrosis/diagnostic imaging , Talus , Technetium Tc 99m Medronate/analogs & derivatives , Technetium , Adult , Humans , Male , Osteonecrosis/etiology , Prognosis , Radionuclide Imaging , Talus/injuries
11.
Biol Reprod ; 26(1): 147-54, 1982 Feb.
Article in English | MEDLINE | ID: mdl-6175352

ABSTRACT

Isolated Golgi apparatus membranes from the germinal elements (spermatocytes and early spermatids) of rat testis were examined for their ability to incorporate [14C]mannose and [14C]galactose into glycolipid and glycoprotein fractions. Transfer of mannose from GDP-[14C]mannose into a Lipid I fractions (GPD:MPP mannosyl transferase activity), identified as mannosyl phosphoryl dolichol, showed optimal activity at 1.5 mM manganese and at pH 7.5. Low concentrations of Triton X-100 (0.1%) stimulated transferase activity in the presence of exogenous dolichol phosphate (Dol-P); however, inhibition occurred at Triton X-100 concentrations greater than 0.1%. Maximal activity of this GDP:MPP mannosyl transferase occurred at 25 microM Dol-P. Activity using endogenous acceptor was 2.34 pmole/min/mg, whereas in the presence of 25 microM Dol-P the specific activity was 284 pmole/min/mg, a stimulation of 125-fold. Incorporation of mannose into a Lipid II (oligosaccharide pyrophosphoryl dolichol) and a glycoprotein fraction was also examined. In the absence of exogenous Dol-P, rapid incorporation into Lipid I occurred with a subsequent rise in Lipid II and glycoprotein fractions suggesting precursor-product relationships. Addition of exogenous Dol-P to galactosyl transferase assays showed only a minor stimulation, less than twofold, in all fractions. Over the concentration range of 9.4 to 62.5 micrograms/ml Dol-P, only 1% of radioactive product accumulated in the combined lipid fractions. These observations suggest that the mannose transfer involves Dol-P intermediates and also that spermatocyte Golgi membranes may be involved in formation of the oligosaccharide core as well as in terminal glycosylations.


Subject(s)
Dolichol Phosphates/pharmacology , Galactosyltransferases/metabolism , Golgi Apparatus/enzymology , Hexosyltransferases/metabolism , Mannosyltransferases/metabolism , Polyisoprenyl Phosphates/pharmacology , Spermatozoa/ultrastructure , Testis/cytology , Animals , Glycolipids/metabolism , Glycoproteins/metabolism , Guanosine Diphosphate Mannose/metabolism , Male , Rats , Rats, Inbred Strains , Spermatids/ultrastructure , Spermatocytes/ultrastructure , Uridine Diphosphate Galactose/metabolism
14.
Drug Metab Dispos ; 5(3): 268-72, 1977.
Article in English | MEDLINE | ID: mdl-17525

ABSTRACT

The effects of delta9-tetrahydrocannabinol (THC) and cannabidiol (CBD) on hydroxylation of estradiol and testosterone in rat liver microsomes were investigated. Acute and chronic treatment of male and female rats with either cannabinoid, 2 or 10 mg/kg, significantly elevated steroid hydroxylase activity. Acute administration of THC or CBD, 10 mg/kg, evoked no detectable changes in cytochrome P-450 levels, but a significant decrease in those of cytochrome b5. Chronic administration of THC or CBD, 2 mg/kg, decreased levels of cytochrome P-450, whereas cytochrome b5 levels appeared normal. Acute doses of THC or CBD at 10 mg/kg significantly depressed testosterone formation in testis microsomes. Chronic THC, 2 mg/kg, but not CBD, evoked the most dramatic decrease in testicular enzyme activity.


Subject(s)
Cannabidiol/pharmacology , Cannabinoids/pharmacology , Dronabinol/pharmacology , Gonadal Steroid Hormones/metabolism , Animals , Cytochrome P-450 Enzyme System/metabolism , Cytochromes/metabolism , Estradiol/metabolism , Female , Hydroxylation , In Vitro Techniques , Male , Microsomes/drug effects , Microsomes/metabolism , Microsomes, Liver/drug effects , Microsomes, Liver/enzymology , Microsomes, Liver/metabolism , Rats , Testis/metabolism , Testis/ultrastructure , Testosterone/biosynthesis , Testosterone/metabolism , Time Factors
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