Clinical experience with a microvascular anastomotic device in head and neck reconstruction.

BACKGROUND: Despite numerous refinements in microsurgical technique and instrumentation, the microvascular anastomosis remains one of the most technically sensitive aspects of free-tissue transfer reconstructions. MATERIALS AND METHODS: Concurrent with the development of microsurgical techniques, various anastomotic coupling systems have been introduced in an effort to facilitate the performance and reliability of microvascular anastomoses. The microvascular anastomotic coupling device (MACD) studied here is a high-density, polyethylene ring-stainless steel pin system that has been found to be highly effective in laboratory animal studies. Despite its availability for human clinical use over the last 5 years, reported clinical series remain rare. Our clinical experience with this MACD in 29 head and neck free-tissue transfers is reported herein. RESULTS: Thirty-five of 37 (95%) attempted anastomoses were completed with 100% flap survival with a variety of donor flaps, recipient vessels, and clinical contexts. Two anastomoses were converted to conventional suture technique intraoperatively, and one late postoperative venous thrombosis occurred after fistulization and vessel exposure. CONCLUSIONS: We conclude that the MACD studied here is best suited for the end-to-end anastomosis of soft, pliable, minimally discrepant vessels. Previous radiation therapy does not appear to be a contraindication to its use. Interpositional vein grafts may also be well suited to anastomosis with the device. When carefully and selectively employed by experienced microvascular surgeons, this MACD can be a safe, fast, and reliable adjunct in head and neck free-tissue transfer reconstructions, greatly facilitating the efficiency and ease of application of these techniques.

A scanning electron-microscopic, stereo-pair study of methacrylate corrosion casts of the mouse palatal and molar periodontal microvasculature.

Microvascular beds of the palate, gingiva and periodontal ligament had interconnected but distinct, regional patterns. The palatal vasculature reflected mucosal-crest morphology: crestal capillary vessels of the rugae anastomosed with sagitally-orientated rows of 8 microns capillary loops, and, in the inter-rugal troughs, these formed a flat plexus overlying collecting veins more than 100 microns in diameter. Maxillary and mandibular molar ligaments had similar microvascular patterns. The molar gingiva had a circular, outer capillary and inner venous system linked by radial anastomoses. The outer (7 microns) capillaries enclosed the three molars in a continuous horizontal loop coursing beneath the crestal epithelium; the inner (10-15 microns) venous vessels encircled each molar just below the epithelial attachment. Glomerulus-like vascular formations, with an arterial and venous stalk, were associated with the inner circular system and extended toward the crevicular epithelium. Axially aligned, post-capillary, periodontal-ligament vessels (21 microns) anastomosed with the inner circular system, forming different patterns in the occlusal, middle and apical thirds. The apical pattern comprised an enveloping plexus of anastomosing venous vessels supplied by arterio-venous shunts; similar shunts were present throughout the ligament. The microvascular bed of the mandibular inter-radicular ligament was characterized by the presence of a large venous ampulla measuring 60 by 200 microns. Some regions of the ligament microvasculature drained via the medullary vessels into 50 microns-diameter venules located interdentally deep to the molar apices. Volumetrically, the ligament microvascular bed was predominantly of post-capillary venules, and morphologically, a paired arterial and venous system was not demonstrated.

Microbial evaluation: 139 implants removed from symptomatic patients.

Possible adverse effects of microbial organisms have been implicated in symptomatic silicone implant patients. In the literature, numerous authors have investigated the possible role of infection with respect to implant problems. To date, various bacterial species have been reported, including Staphylococcus aureus, Staphylococcus epidermidis, peptostreptococci, and Clostridium perfringens. Infections in polyurethane-coated prostheses also have been shown to prolong morbidity. Antibiotic use has been relatively empirical in this regard. The purpose of this study was, first, to determine the frequency, type, and clinical relevance of microbial colonization on implant surfaces removed from symptomatic patients and, second, to determine possible effects of microbial colonization on implant integrity (gel bleed, rupture). A total of 139 implants from 72 symptomatic patients were entered into the prospective clinical study between February of 1993 and July of 1994 at the UCLA Medical Center. The implant shell types included smooth (79 percent), polyurethane (8 percent), textured (7 percent), and smooth and Dacron (6 percent). The implant locations were subglandular (71 percent), submuscular (28 percent), and subcutaneous (1 percent). Of the 139 implants removed, 69 percent were intact and 31 percent were ruptured. Forty-seven percent of 139 implants were culture-positive. Propionibacterium acnes was isolated most frequently (57.5 percent), followed by Staphylococcus epidermidis (41 percent), and then Escherichia coli (1.5 percent). No fungal infections were identified. Culture positivity was not significantly associated with systemic symptoms. Sixty-seven percent of the positive culture implants were intact; 33 percent were ruptured. The frequency (47 percent) and types (P. acnes and S. epidermidis) of microbial colonization are determined in symptomatic silicone implant patients.

The primary structure of a salivary calcium-binding proline-rich phosphoprotein (protein C), a possible precursor of a related salivary protein A.

The complete primary structure of a calcium-binding "proline-rich phosphoprotein" named salivary Protein C was determined from peptides obtained by enzymatic and chemical cleavages of the protein. The protein consists of a single polypeptide chain of 150 residues. It contains the entire primary structure of a previously isolated salivary Protein A in its NH2-terminal 106 residues. The COOH-terminal 44 residues consist mostly of glycine, glutamine, and proline, including a hexaproline sequence, but no polyproline structure could be detected by CD spectroscopy. There is extensive repetition of sequences in the protein, suggesting gene multiplication and recurrent folding. Comparison of the primary structure of salivary Proteins A and C with known protein sequences indicate that the salivary proteins constitute a new family. A mouse submaxillary protease will cleave salivary Protein C between residues 106 and 107 only, giving rise to salivary Protein A and a 44-residue COOH-terminal peptide. This cleavage and the sequence data suggest that salivary Protein C may be a precursor of salivary Protein A.

The role of glandular kallikrein in the formation of a salivary proline-rich protein A by cleavage of a single bond in salivary protein C.

An enzyme was purified from human parotid saliva that can cleave a single arginine-glycine peptide bond between residues 106 and 107 in human salivary proline-rich protein C, hereby giving rise to another proline-rich protein A, which is also found in saliva. The enzyme was purified 2400-fold. It cleaved salivary protein C at the rate of 59 micrograms of protein/h per microgram of enzyme and had amino acid composition, molecular weight and inhibition characteristics similar to those reported for human salivary kallikrein. Confirmation that the enzyme was kallikrein was demonstrated by its kinin-generating ability. Histochemical evidence indicates that a post-synthetic cleavage of protein C by kallikrein would have to take place during passage of saliva through the secretory ducts. In secreted saliva, cleavage of salivary protein C can only be observed after 72 h incubation. In addition, there is no effect of salivary flow rate on the relative amounts of proteins A and C in saliva. On the basis of the experimental observations, it is proposed that in vivo it is unlikely that kallikrein secreted from ductal cells plays a significant role in converting protein C into protein A.