Epidural Idiopathic Sterile Pyogranulomatous Inflammation Causing Spinal Cord Compressive Injury in Five Miniature Dachshunds

Objective— To characterize the clinical signs, diagnostic and surgical findings, and outcome of dogs with idiopathic sterile pyogranulomatous inflammation (ISP) of epidural fat causing spinal cord compression.
Study Design— Retrospective study.
Animals— Dogs (n=5).
Methods— Dogs with epidural ISP (2002–2006) were identified retrospectively. Inclusion criteria were neurologic examination, myelography, and definitive diagnosis of ISP confirmed by surgery and histopathologic examination of epidural spinal cord compressive tissue.
Results— The most common clinical sign was paraparesis/paraplegia. No abnormalities were detected by laboratory testing or survey spine radiographs. On myelography, extradural spinal cord compressions were focal (dogs 1, 3, and 5) or multifocal (dogs 2 and 4). Surgical decompression of the spinal cord was completed by hemilaminectomy. Epidural fat collected surgically had pyogranulomatous inflammation of unknown cause and was histologically similar to subcutaneous ISP. All dogs had good long-term neurologic outcome (10–45 months follow-up). Some dogs had episodes of ISP at other sites before or after surgical treatment of epidural ISP, suggesting there may be a systemic form of ISP.
Conclusion— Epidural ISP may cause a spinal cord compressive lesion in Miniature Dachshunds, which can be treated by surgical decompression of the spinal cord with or without administration of adjunctive steroids.
Clinical Relevance— Epidural ISP should be considered as a possible cause of thoracolumbar myelopathy for Miniature Dachshunds.     

Immunological detection of translation products of type V/XI collagen α1 gene and their degradation products in red sea bream muscle

We previously cloned cDNA of type V/XI collagen α1 chain (ColVa1) gene from cultured cells derived from red sea bream embryo. We raised an antibody against the deduced C-telopeptide of ColVa1 in order to detect the translation products of this cDNA and their degradation products in red sea bream muscle. To improve its specificity, the antibody was purified from rabbit antiserum by use of an affinity column cross-linked with recombinant C-terminal peptide of ColVa1 produced by Epicurian coli. The purified antibody recognized a band corresponding to the α chain of type V/XI collagen in western blot analysis of the extract of cultured cells. The antibody also recognized two bands in acid-soluble and pepsin-solubilized collagens, indicating that the translation products of the ColVa1 gene are present in muscle and that bands correspond to α and β chains of type V/XI collagen. A band corresponding to a molecular weight of approximately 65 k was detected in the NaOH extracts of muscle, suggesting that type V/XI collagen α1 chain is restrictedly digested in red sea bream muscle.