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Effects of 1alpha,25 dihydroxyvitamin D3 on the expression of HO-1 and GFAP in glial cells of the photothrombotically lesioned cerebral cortex.
PMID 15531134
Abstract In ischemic cerebral injuries a cascade of degenerative mechanisms, all participating in the development of oxidative stress, influence the condition of the tissue. The survival of viable tissue affected by secondary injury largely depends on the balance between endogenous protective mechanisms and the ongoing degenerative processes. The inducible enzyme, heme oxygenase-1 metabolizes and thus detoxifies free heme to the powerful endogenous antioxidants biliverdin and bilirubin therefore enhancing neuroprotection. The secosteroid 1alpha,25-dihydroxyvitamin D3 (1,25-D3) is a modulator of the immune system and also exhibits a strong potential for neuroprotection as recently shown in the MCAO model of cerebral ischemia. We studied the effects of 1,25-D3 treatment on heme oxygenase-1 expression following focal cortical ischemia elicited by photothrombosis. Postlesional treatment with 1,25-D3 (4 microg/kg body weight) resulted in a transient, but significant upregulation of glial heme oxygenase-1 immunoreactivity concomitant with a reduction in glial fibrillary acidic protein immunoreactivity in remote cortical regions affected by a secondary spread of injury, whereas the size of the lesion's core remained unaffected. 1,25-D3 did not produce a temporal shift or extension of injury-related heme oxygenase-1 responses, indicating that 1,25-D3 did not prolong ischemia-related heme oxygenase-1 expression. In contrast to glial heme oxygenase-1 upregulation, glial fibrillary acidic protein, a sensitive marker for reactive gliosis, was significantly reduced. These findings support an additional protective action of 1,25-D3 at the cellular level in regions affected by secondary injury-related responses.
Authors Karl Zilles , Otto-W Witte , Hans-J Bidmon , Evelyn Oermann
Journal Title Journal of chemical neuroanatomy

By red staining for collagen and using unpolarized and polarized light, he saw that there is less collagen 1 type fibers in the MS jugular vein tissue, and more collagen III fibers in MS. This is the exact opposite of the controls.

Connective tissue in MS switches from collagen I to collagen III and this takes place in the IJVs. This switch also happens in fibromatosis, colloids and hypertrophied scars, and this remodeling may play a role in CCSVI disturbances

Comparison of collagen subtype I and III presence in varicose and non-varicose vein walls.

Haviarova Z, Janega P, Durdik S, Kovac P, Mraz P, Stvrtinova V.

Institute of Anatomy, Faculty of Medicine, Comenius University, Bratislava, Slovakia. zora.haviarova@fmed.uniba.sk

STUDY OBJECTIVES: The connective tissue alterations in varicose vein wall are supposed to be one of the main causes of primary varicose vein (main sign of human lower limbs chronic venous insufficency). METHODS: 5 varicose vein samples from 5 patients undergoing stripping surgery of long saphenous vein were compared with 5 control samples of healthy (non-dilated) long saphenous veins from necroptic material (with no history of varicosis). They were fixed in a Baker solution, processed by use of light microscopic method, cut to ultra-thin sections (4-5 microm) and stained with PicroSirius Red for collagen. Sections were scanned with light microscope (Leica, Germany) and camera Canon S50 (Germany) and analysed by morphometric programme Image J v.1.38g (National Institute of Health, USA). RESULTS: In the group of healthy (non-dilated) veins the mean collagen I/III ratio value was 31.40 and in the group of varicose veins the mean collagen I/III ratio was 12.35; the difference is statistically significant: healthy veins contain significantly more of collagen subtype I and varicose veins contain significantly more of collagen subtype III in their walls. CONCLUSION: The statistically significant difference in the collagen I/III ratio between the groups of healthy (non-dilated) and varicose (dilated) vein walls is worthy of further following (Tab. 2, Fig. 7, Ref. 12). Full Text (Free, PDF) www.bmj.sk.

Haviarova Z, Janega P, Durdik S, Kovac P, Mraz P, Stvrtinova V.

Institute of Anatomy, Faculty of Medicine, Comenius University, Bratislava, Slovakia. zora.haviarova@fmed.uniba.sk