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Biomedical subjects

L T Jensen

Publications and source records attributed to L T Jensen.

66 records · Page 4Linked to original sources

Serum aminoterminal type III procollagen peptide reflects repair after acute myocardial infarction.

In 16 patients with acute myocardial infarction and in 15 controls, procollagen type III aminoterminal peptide in serum (PIIINP) was measured consecutively. Serum PIIINP was increased on the second to third postinfarction day (p less than 0.01) and remained elevated for more than 4 months. Peak values were observed on the third to seventh postinfarction day. The individual peak changes were correlated to infarction size calculated from serum CK-MB and serum lactate dehydrogenase (p = 0.60, p = 0.02). The changes in distribution of PIIINP-related antigens in serum after gel chromatography were similar to changes observed during wound healing in humans. PIIINP is cleaved off procollagen type III during the biosynthesis of type III collagen, which characterizes the early stages of repair and inflammation. Our findings suggest that serum PIIINP reflects the repair processes and scar formation following acute myocardial infarction. The serum PIIINP alterations in acute myocardial infarction differ essentially from the changes in myocardial enzymes reflecting myocardial injury. Serum PIIINP may therefore provide new and clinically relevant information on the healing of myocardial infarction.

Adult↗

External thoracic duct-venous shunt in conscious pigs for long term studies of connective tissue metabolites in lymph.

An experimental animal model for lymph studies is described. Thoracic duct-venous shunt was established in 12 pigs. Shunt patency averaged 5.5 days. The composition of connective tissue metabolites in lymph and serum were investigated during a standardized surgical operation (thoracotomy) under general anesthesia. We measured the carboxyterminal propeptide of type I procollagen (PICP), the aminoterminal propeptide of type III procollagen (PIIINP) hyaluronan (HA) and total protein. During surgery/anesthesia lymph PICP (p less than 0.04), lymph PIIINP (p less than 0.03) and serum PIIINP (p less than 0.01) and serum PIIINP (p less than 0.03) increased. The changes may be explained by the inactive physical state of the animals. HA showed wide variations, with a tendency like PIIINP. In conscious animals the lymph/serum ratio of PIIINP and HA were 10 and 35, respectively, indicating that lymph is a major route of tissue clearance for these components. The lymph/serum ratio of PICP was 1.0 in conscious pigs, indicating a direct release into the circulation. Total protein in lymph decreased (p less than 0.04) during surgery/anesthesia, whereas no changes were observed in serum. Pigs can be used instead of dogs and sheep in studies on lymph. The effect of surgery/anesthesia must be taken into consideration.

Anastomosis, Surgical↗

Procollagen type-III aminoterminal peptide in serum and synovial fluid of dogs with hip dysplasia and coxarthrosis.

Hip dysplasia is an affection of the coxofemoral joint that progresses until stabilization is caused by fibrosis and osteoarthritic changes. This stabilization process can be examined by clinical and radiographic methods. The capability of evaluating the procollagen concentrations in liquids, such as serum and synovial fluid, has further offered the basis for an objective biochemical evaluation of the stabilization process. Our study was performed to evaluate whether determination of procollagen concentrations was suitable for the use in practice. The procollagen type-III aminoterminal peptide (P-III-NP) concentration was measured in serum and in synovial fluid from coxofemoral joints in 20 dogs. Dogs were grouped on the basis of evidence of dysplasia and osteoarthritic changes of the hip: (1) a control group of 6 dogs without clinical or radiographic signs of hip dysplasia, and (2) dysplastic group of 14 dogs, which was further grouped with respect to the coxofemoral joint laxity, as determined by the Ortolani test. Synovial fluid concentration of P-III-NP was significantly (P less than 0.05) higher in fluid from dysplastic joints than in fluid from normal joints. Serum concentrations of P-III-NP were significantly (P less than 0.05) higher in dogs in which results of the Ortolani test were positive.

Animals↗

Circulating connective tissue metabolites in patients with bancroftian filariasis.

Sera from adults from an area of Tanzania with high endemicity for Wuchereria bancrofti infection were examined for 4 serological markers of extracellular matrix activity, namely the amino-terminal propeptide of type III procollagen (PIIINP), the carboxy-terminal propeptide of type I procollagen (PICP), the carboxy-terminal telopeptide of type I collagen (ICTP), and hyaluronan. Sera from individuals with non-filarial elephantiasis and from healthy Danes were included as controls. No association was observed between the mean serum concentration of PIIINP or PICP and the clinical, microfilarial or circulating filarial antigen status of the individuals. The mean concentration of ICTP was significantly higher (P < 0.01) in sera from individuals with filarial and non-filarial elephantiasis than in sera from individuals living in filariasis endemic areas but without elephantiasis or in the Danish control sera. Among individuals from the filariasis endemic area, the mean serum concentration of hyaluronan was significantly higher (P < 0.01) in microfilaraemic than in amicrofilaraemic individuals, and significantly higher (P < 0.01) in individuals who had circulating filarial antigens than in those who did not, but there was no relation to the clinical status. The significance of the findings are discussed in relation to the pathological processes taking place in bancroftian filariasis.

Adolescent↗

Human monocyte elastolytic activity, the propeptides of types I and III procollagen, proteoglycans, and interleukin-6 in synovial fluid from patients with arthritis.

Elastolytic activity by live human monocytes (M phi) is mainly caused by cell surface related leucocyte elastase, capable of degrading matrix components. In order to examine the possible correlation between enzyme activity and tissue turnover in the joint, we examined 24 synovial fluids for M phi elastolytic activity, using the levels of synovial fluid interleukin-6 and serum C reactive protein as additional markers of cell activation. Proteoglycan levels were measured as an indication of cartilage degradation and the types I and III procollagen propeptides as markers of synovial membrane turnover. We found that elastolysis by live M phi and the levels of interleukin-6 and C reactive protein correlated significantly with proteoglycan concentrations but not with the procollagen propeptides. These findings suggest that human M phi elastolytic activation is a biologically relevant factor in cartilage degradation, but is unrelated to the collagen metabolism of the synovial membrane.

Adult↗

Nine pheochromocytomas in the same patient. Final mapping with ultrasound and angiography.

A 37-year-old man presented with hypertension and elevated urine catecholamine. Ultrasound scanning revealed a solid tumour of the right adrenal gland and two solid tumours in the retroperitoneum. The findings were confirmed with computed tomography and abdominal angiography. At surgery only the tumour of the right adrenal gland was removed. The histopathologic diagnosis was pheochromocytoma. Postoperatively the symptoms and biochemistry were unchanged and the patient was referred for further treatment. At ultrasonography and abdominal aortography 6 remaining tumours were demonstrated. Surgery was performed and 8 pheochromocytomas were extirpated (3 were closely spaced small tumours in a conglomerate corresponding to one of the visualized tumour sites). On histopathologic examination no signs of invasive growth were found. The patient recovered completely. The blood pressure was still normal 2 1/2 years later. Angiography and non-invasive examination of the entire abdomen and pelvis should be routine when pheochromocytomas are searched for.

Adrenal Gland Neoplasms↗