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1.
Ann Plast Surg ; 42(3): 330-2, 1999 Mar.
Article in English | MEDLINE | ID: mdl-10096627

ABSTRACT

The authors describe an uncommon case of flexor tenosynovitis caused by Mycobacterium terrae, an atypical mycobacterium generally considered nonpathogenic in humans. A prolonged delay in diagnosis and various ineffective therapies led to synovial biopsy and culture. After confirming the diagnosis of M. terrae, appropriate antimycobacterial chemotherapy resolved the synovitis. For chronic tenosynovitis without a clear etiology, limited synovectomy and culture are essential in establishing a diagnosis and in initiating treatment for this atypical mycobacterial infection.


Subject(s)
Hand/microbiology , Mycobacterium Infections/diagnosis , Mycobacterium/isolation & purification , Tenosynovitis/microbiology , Adult , Hand/pathology , Hand/surgery , Humans , Male , Mycobacterium Infections/pathology , Mycobacterium Infections/surgery , Tenosynovitis/pathology , Tenosynovitis/surgery
2.
Kidney Int ; 43(6): 1371-6, 1993 Jun.
Article in English | MEDLINE | ID: mdl-8315952

ABSTRACT

We have recently demonstrated elevations of separate amino- and carboxy-terminal parathyroid hormone-related protein (PTHrP) fragments in patients with humoral hypercalcemia of malignancy (HHM) using both a two-site immunoradiometric assay (IRMA) with amino-terminal specificity for PTHrP, and with a carboxy-terminal radioimmunoassay (RIA) for PTHrP(109-138). PTHrP(109-138) immunoactivity from plasma of patients with HHM could not be extracted using an amino-terminal PTHrP immunoaffinity column, indicating that the carboxy-terminal region circulates as a discrete peptide. Carboxy-terminal immunoreactive (i) PTHrP levels were also elevated in normocalcemic patients with chronic renal failure (without cancer), whereas amino-terminal iPTHrP levels were normal in patients with renal failure. In order to further define the renal handling of carboxy-terminal PTHrP peptides, we have evaluated circulating iPTHrP(109-138) concentrations in patients with a wide range of renal function. We studied 25 patients with abnormal renal function of diverse etiologies whose creatinine clearances ranged from 66 ml/min to less than 5 ml/min. All patients had undetectable or low (< or = 2 pmol/liter) concentrations of iPTHrP(1-74). iPTHrP(109-138) concentrations were undetectable in patients with creatinine clearances > or = 20 ml/min, but became elevated in patients with creatinine clearances < 20 ml/min. The log of iPTHrP(109-138) correlated negatively with the log of creatinine clearance (r = 0.88, P = 0.0001). Mean iPTHrP(109-138) levels were slightly higher for patients on hemodialysis (32.7 +/- 3.1 pM) than for those on chronic ambulatory peritoneal dialysis (22.1 +/- 3.4 pM; P < 0.05), suggesting that some carboxy-terminal PTHrP fragments may be cleared to a greater extent by the peritoneal membrane.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Parathyroid Hormone/blood , Peptide Fragments/blood , Peptide Fragments/metabolism , Proteins/metabolism , Renal Insufficiency/blood , Animals , Chromatography, Gel , Humans , Hypercalcemia/blood , Parathyroid Hormone-Related Protein , Rabbits
3.
J Clin Endocrinol Metab ; 75(4): 1110-4, 1992 Oct.
Article in English | MEDLINE | ID: mdl-1400879

ABSTRACT

PTH-related peptide (PTHrP) immunoreactivity in plasma from six well characterized patients with humoral hypercalcemia of malignancy was characterized by gel filtration chromatography. An immunoradiometric assay directed against the N-terminal 74 amino acids of PTHrP and a RIA directed against the C-terminal region (amino acids 109-138) of the peptide were used to assay column fractions. When examined using acid (pH 5.0) nondenaturing conditions, N-terminal PTHrP immunoreactivity eluted with an apparent M(r) of 30,000-40,000. The apparent M(r) of this PTHrP fragment shifted to approximately 25,000 when gel filtration was performed at pH 9.0. The apparent M(r) shifted further, to approximately 6,500, when chromatographed under denaturing conditions in 4 M guanidine-HCl. Carboxy-terminal PTHrP immunoreactivity in plasma eluted with an M(r) of approximately 12,000 under acid nondenaturing conditions, as did the synthetic C-terminal PTHrP column marker, PTHrP (109-138). Synthetic PTHrP (1-36) and (1-74), and recombinant PTHrP (1-141) as well as native PTHrP species found in milk and keratinocyte-conditioned medium migrated in their expected positions when analyzed under alkaline nondenaturing or under denaturing condition. We conclude that native, synthetic, and recombinant PTHrP peptides may migrate anomalously when examined using gel filtration under nondenaturing conditions, and such studies should be interpreted with caution. Plasma from patients with humoral hypercalcemia of malignancy contains at least two PTHrP species. One native N-terminal fragment appears, as assessed under denaturing conditions, to have an M(r) of approximately 6,500, and to therefore comprise approximately 50-60 amino acids of full-length PTHrP. A second chromatographically and immunologically distinct C-terminal fragment with an M(r) of approximately 12,000 under nondenaturing conditions is also present.


Subject(s)
Hypercalcemia/blood , Neoplasm Proteins/blood , Paraneoplastic Syndromes/blood , Parathyroid Hormone-Related Protein , Peptide Fragments/metabolism , Proteins/metabolism , Chromatography, Gel , Female , Humans , Hypercalcemia/etiology , Immunoradiometric Assay , Protein Denaturation
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