Successful prosthetic fitting of a 73-year-old hip disarticulation amputee patient with cardiopulmonary disease.

Patients with hip disarticulation (HD) require high energy expenditure for successful prosthetic ambulation. Thus, older patients are rarely fitted with an HD prosthesis. To our knowledge there are no reports of gait analysis following successful prosthetic fitting of an elderly HD amputee patient with systemic cardiopulmonary disease. We report the case of successful prosthetic ambulation in a 73-year-old man with HD secondary to histiosarcoma and a medical history significant for stable angina, chronic obstructive pulmonary disease, and diabetes mellitus. The patient underwent gait training with an endoskeletal prosthesis and achieved ambulation to 400 feet with bilateral forearm crutches. Vicon kinematic gait analysis revealed a cadence of 44 steps/min (112 steps/min normal), and double support time of 47% (26% normal). Oxygen rate during ambulation (VO2) was 11.0 mL/kg/min at velocity of .35 m/sec, compared with published figures for ambulation in those with HD of 10.73 mL/kg/min at velocity of .93 m/sec. At 1-year follow-up, the patient continued to walk into church with the prosthesis. We conclude that a trial fitting of an HD prosthesis should be considered on an individual basis in elderly amputee patients.

Evolutionary and structural relationships among the group-specific component, albumin and alpha-fetoprotein.

The group-specific component (Gc) is a plasma protein that binds vitamin D. Recent characterization of human Gc cDNA demonstrated homology with serum albumin and alpha-fetoprotein. This study compares the sequences of the three proteins and demonstrates a strong evolutionary relationship. Albumin, alpha-fetoprotein and Gc evolved from an ancestral gene containing an intragenic triplication. Comparison of the amino acid sequences and patterns of double disulfide bonds suggests that the Gc gene may have diverged from an ancestral gene earlier in evolution than the genes encoding albumin and alpha-fetoprotein. Analysis of the amino acid and nucleotide sequences of the three internal domains of Gc revealed 19-23% amino acid sequence identity and the localization of three homology blocks with 40-44% nucleotide sequence identity. The deduced amino sequence of Gc furnished data for comparing its molecular configuration based on the predicted secondary structure with those predicted for human albumin and alpha-fetoprotein. Utilization of Gc cDNA has also led to the identification of its genomic DNA and detection of a human DNA polymorphism.