Management of separation pain after single-dose methotrexate therapy for ectopic pregnancy.

OBJECTIVE: To evaluate the conservative management of pain after systemic methotrexate therapy for ectopic pregnancy; identify prognostic factors for success; and compare hCG resolution time for patients with and without pain. METHODS: A retrospective review of patients with ectopic pregnancy requiring evaluation for pain after receiving single-dose methotrexate therapy is performed. Results of hematocrits, ultrasound findings, hCG levels, time for hCG levels to reach less than 15 mIU/mL, and outcome were noted. RESULTS: Fifty-three patients with 64 episodes of pain were identified. Seven hospitalized patients required surgery during admission. Two previously hospitalized and one outpatient also ultimately underwent surgery. For hospitalized patients, there were no statistical differences between patients who did or did not undergo surgery during admission for any variable studied, including the presence of free peritoneal blood or rebound tenderness. However, comparison of hospitalized and nonhospitalized patients showed those with rebound tenderness were more likely to be admitted. Hospitalized patients not requiring surgery had shorter resolution time than nonhospitalized patients. For hospitalized and nonhospitalized patients, the median time from treatment to presentation for pain was 8 days. CONCLUSION: The occurrence of pain following methotrexate therapy for ectopic pregnancy should not be the sole indication for surgical intervention. The majority of stable patients with pain after methotrexate therapy, even with rebound or free peritoneal fluid, can be treated successfully without surgery, either in hospital with close observation for severe pain or as outpatients for patients with less severe pain.

Further characterization of the loop structure of platelet glycoprotein IIIa: partial mapping of functionally significant glycoprotein IIIa epitopes.

Glycoprotein (GP) IIb-IIIa serves as the platelet fibrinogen receptor. Studies of the tertiary structure of GPIIIa have shown that the protein has a large loop structure of at least 325 amino acids in length. To further characterize this loop structure, intact platelets were digested with alpha-chymotrypsin. Digestion products were examined using the anti-GPIIIa monoclonal antibodies (MoAbs) AP3, D3GP3, and C5GP3, as well as the human alloantibody, anti-PLA1. AP3 recognized GPIIIa digestion products of 109, 95, and 68 Kd. D3GP3 and C5GP3 recognized an additional band of 51 Kd. Time course digestions demonstrated that the 51-Kd fragment was generated by proteolysis of the 68-Kd peptide. Sequence analysis of the reduced 51-Kd peptide showed that this fragment began at amino acid 422. The nonreduced 51-Kd peptide was reactive with antibodies directed against the first 13 amino acids of GPIIIa, demonstrating the presence of a covalently attached N-terminal peptide. These data suggest that: (1) the minimum length of the loop structure is at least 384 amino acids; (2) the AP3 epitope is formed at least in part by a determinant contained within residues 348 to 421; and (3) the D3GP3 and C5GP3 epitopes are contained within amino acids 422 to 692 of GPIIIa, a region that may be flexible and involved in conformational changes that occur after ligand binding.