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1.
Sportverletz Sportschaden ; 25(3): 173-8, 2011 Sep.
Article in German | MEDLINE | ID: mdl-21922440

ABSTRACT

AIM: Femoroacetabular impingement (FAI) is a recently proposed mechanical concept for the development of osteoarthritis of the hip. Aim of this nationwide survey is the description of the current status of diagnostics and therapy of FAI in Germany. MATERIAL AND METHODS: All orthopedic and traumatological hospitals listed in the "list of German hospitals 2006" were invited via e-mail to take part in this anonymous survey. RESULTS: The questionnaire was answered by 682 departments (50.5 %). 98 (14.3 %) of these departments treated FAI in 2007. CONCLUSION: In Germany, diagnostics and treatment of FAI were performed inconsistently in a small number of specialized hospitals.


Subject(s)
Femoracetabular Impingement/diagnosis , Femoracetabular Impingement/surgery , Adult , Aged , Arthroscopy , Cross-Sectional Studies , Female , Femoracetabular Impingement/etiology , Germany , Health Surveys , Hospitalization/statistics & numerical data , Humans , Internet , Male , Middle Aged , Minimally Invasive Surgical Procedures , Osteoarthritis, Hip/diagnosis , Osteoarthritis, Hip/epidemiology , Osteoarthritis, Hip/surgery , Postoperative Care , Surveys and Questionnaires
3.
Biochim Biophys Acta ; 982(1): 140-6, 1989 Jun 26.
Article in English | MEDLINE | ID: mdl-2472836

ABSTRACT

Lysophospholipids inhibited mitochondrial Ca2+ uptake, induced a net Ca2+ efflux, and thereby increased the extramitochondrial Ca2+ concentration. The inhibitory potency decreased in the order lysophosphatidylcholine (LPC) = lysophosphatidylglycerol (LPG) greater than lysophosphatidylinositol (LPI) greater than lysophosphatidylserine (LPS) much greater than lysophosphatidylethanolamine (LPE). This relative order is in inverse relation to the ability of the various phospholipid head-groups to build up intermolecular hydrogen bonds with neighbouring membrane lipids. This indicates that changes in Ca2+ transport induced by lysophospholipids are mediated by the interaction of the lysophospholipids with the mitochondrial membrane bilayer structure. The mitochondrial membrane potential, which is the main driving force for mitochondrial Ca2+ uptake, was affected in the same order by the various lysophospholipids. This reduction of the mitochondrial membrane potential may be the underlying cause for the inhibition of the mitochondrial Ca2+ uniport and the resulting release of Ca2+ from the mitochondria.


Subject(s)
Calcium/metabolism , Mitochondria, Liver/metabolism , Phospholipases A/metabolism , Phospholipases/metabolism , Animals , Biological Transport/drug effects , In Vitro Techniques , Intracellular Membranes/physiology , Lysophosphatidylcholines/pharmacology , Lysophospholipids/pharmacology , Membrane Potentials/drug effects , Phospholipases A2 , Rats , Rats, Inbred Strains , Ruthenium Red/pharmacology , Sodium/pharmacology , Structure-Activity Relationship
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